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Department of Genetics

Head: Professor Teresa Żołądek

Department of Genetics consists of six research groups working on different topics.
Four groups are using yeast Saccharomyces cerevisiae as a model organism to study various aspects of cell genetics and physiology: genetic regulation of metabolism (dr hab. Róża Kucharczyk), mechanisms of protein transport (prof. Teresa Żołądek), regulation of tRNA transcription (prof. Magdalena Rakowska-Boguta) and mechanisms of cell division (dr hab. Anna Kurlandzka). One group (prof. A. Paszewski) is using filamentous fungus Aspergillus nidulans and yeast cells to study genetic control of sulfur metabolism and one group (dr hab. Beata Burzyńska) is performing genetic analysis of some hereditary human diseases and is using yeast as a model to analyze function of some human genes.

Regulation of tRNA transcription in yeast

Group leader: Prof. Magdalena Boguta
Staff:  Małgorzata Cieśla (PhD),  Ewa Leśniewska (Ph.D. student), Marta Płonka (Ph.D. student)


The leader of new group :  Dr. Damian Graczyk.  Staff: Aneta Jurkiewicz (Ph.D. student), Olga Wojnowska (Ph.D. student)
tRNAs, essential components of the biosynthetic machinery, are synthesized by RNA polymerase III (Pol III). Transcription of tRNA is tightly coupled with cell growth and metabolism. This control is mediated by Maf1, a global negative regulator conserved from yeast to man. Yeast Maf1 was originally found in our laboratory and subsequently shown to function as a repressor of tRNA synthesis. Maf1 mediates various stress signals to Pol III Studies in foreign laboratories provided compelling evidence that Maf1 is also a principle regulator of Pol III in humans, flies, worms and plants.

After discovering the Maf1 function as Pol III repressor in yeast, our study concentrated on deciphering the mode of Maf1 control by environmental conditions. We established that under repressive conditions Maf1 is activated by dephosphorylation and imported to the nucleus. There, hypophosphorylated Maf1 binds to the Pol III complex leading to decreased association of Pol III with chromatin. Alternatively, we have shown that under favorable growth conditions, Maf1 is inactivated by phosphorylation. Apart from decreasing direct binding of Maf1 to Pol III, phosphorylation also facilitates Maf1 export from the nucleus by the Msn5 exportin. Several different kinases, PKA, Sch9, TORC1, CK2, perform these functions by phosphorylating Maf1. We documented that Maf1 interacts with and is subject to CK2 phosphorylation which appears to counteract repression.






Little is known about the biogenesis pol II complex which consists of 17 subunits. We identified a new Pol III assembly factor, Rbs1 which interacts with Pol III and facilitates its import to the nucleus.
Our recent studies focused on the molecular connection between tRNA transcription and regulation of yeast metabolism. Besides elevated tRNA transcription, Maf1-depleted yeast cells manifest the inability to grow on a non-fermentable carbon source. We found that transcription of two major genes controlling gluconeogenesis was decreased in the absence of Maf1. We have also documented a novel direct relationship between Pol III–mediated transcription and fructose 1,6-bisphosphate aldolase, a glycolytic enzyme essential for cell viability.
Synthesis of rRNA and most cellular mRNAs is known to be coupled with various processing events. Yeast tRNAs, generated by Pol III, are processed in the nucleus at the 5’ and 3’ termini, then exported to the cytoplasm, spliced and used in translation on cytoplasmic ribosomes. By examining largely unexplored connections between tRNA transcription and processing, we have shown that Maf1 affects indirectly both, maturation and stability of tRNAs. We were able to show that such pre-tRNA accumulation could be partially overcome by overproduction of tRNA-exportin Los1, suggesting saturation of the tRNA export machinery by the increased amount of pre-tRNA produced in cells lacking Maf1. We also detected connection between Pol III transcription and tRNA decay showing that inhibition of tRNA synthesis suppressed the degradation of hypomodified tRNAVal. Additionally we documented control of S.cerevisiae pre-tRNA processing by environmental conditions.
Recently Dr. Damian Graczyk established a new team and organized a laboratory for studying human cells in cultures. His study is focused on the regulation of RNA polymerase III transcription and its role in mammalian cell physiology.  The current projects directed by Dr. Graczyk  aim to decipher the role of RNA polymerase III in inflammation and colorectal cancer.  


Current Research Grants:


"The role of POLR1D, a common subunit of RNA polymerases I and III, in colorectal cancer". (Foundation for Polish Science, Project FIRST TEAM) 
Principal investigator: dr Damian Graczyk

2016 – 2018

„Regulation of RNA polimerase III in macrophages” (National Science Centre in Cracov, Project Sonata).
Principal investigator: dr Damian Graczyk

2015 - 2017

„Control of tRNA biogenesis” Foundation for Polish Science, Project MISTRZ)
Principal investigator: Magdalena Boguta


"tRNA transcription novel layers of regulation" (National Science Centre in Cracov, Project Maestro; UMO-2012/04/A/NZ1/00052)
Principal investigator: Magdalena Boguta


“Investigation of interplay of tRNA transcription, processing and decay in yeast Saccharomyces cerevisiae" (National Science Centre in Cracov, Project Preludium, 2013/09/N/NZ1/00129)
Principal investigator: Dominika Wichtowska


"Coupling of polymerase III activity and glucose metabolism in yeast Saccharomyces cerevisiae" (National Science Centre in Cracov, N301693740)
Principal investigator: Magdalena Boguta


"PhD programme in Molecular Biology: Studies of nucleic acids and proteins - from basic to applied research" (Foundation for Polish Science, Project MPD 2009-3/2)
Project coordinator: Magdalena Boguta


“New proteins implicated in regulation of tRNA transcription in the yeast Saccharomyces cerevisiae” (Foundation for Polish Science, Project Pomost 2010-2/2)
Principal investigator: Małgorzata Cieśla


Recent publications:

  1. FORETEK D., NUC P.,  ZYWICKI M., KARLOWSKI W., KUDLA G., BOGUTA M. Maf1-mediated regulation of yeast RNA polymerase III is correlated with CCA addition at the 3 ' end of tRNA precursors. Gene (2017) 612: 12-18
  2. LESNIEWSKA E., BOGUTA M. Novel layers of RNA polymerase III control affecting tRNA gene transcription in eukaryotes. Open Biology (2017): 7, 170001
  3. FORETEK D., WU J., HOPPER A.K., BOGUTA M.  Control of S. cerevisiae  pre-tRNA processing by environmental conditions. RNA  Journal (2016) 22: 349-359
  4. TUROWSKI T., LESNIEWSKA E., DELAN-FORINO C., BOGUTA M., TOLLERVEY D. Global analysis of transcriptionally engaged yeast RNA polymerase III reveals extended tRNA transcripts. Genome Research (2016) 26: 933-944
  5. BOGUTA M. Why Are tRNAs Overproduced in the Absence of Maf1, a Negative Regulator of RNAP III, Not Fully Functional?” PLOS Genetics (2015)  11: e1005743
  6. CIESLA M., MAKALA E., PLONKA M., BAZAN R., GEWARTOWSKI K., DZIEMBOWSKI A., BOGUTA M. Rbs1, a New Protein Implicated in RNA Polymerase III Biogenesis in Yeast Saccharomyces cerevisiae. Molecular and Cellular Biology (2015) 35: 1169-1181
  7. LONG J.S., SCHOONEN P.M., GRACZYK D., O'PREY J., RYAN K.M. p73 engages A2B receptor signalling to prime cancer cells to chemotherapy-induced death. Oncogene (2015) 34:5152-5162
  8. GRACZYK D, WHITE RJ, RYAN KM. Involvement of RNA Polymerase III in immune responses. Molecular and Cellular Biology (2015) 35:1848-1859
  9. CIESLA M., MIERZEJEWSKA J., ADAMCZYK M., ÖSTLUND-FARRANTS A., BOGUTA M. Fructose bisphosphate aldolase is involved in the control of RNA polymerase III-directed transcription. Biochimica et Biophysica Acta- Molecular Cell Research (2014) 1843: 1103-1110
  10. WICHTOWSKA D., TUROWSKI T., BOGUTA M. An interplay between transcription, processing, and degradation determines tRNA levels in yeast. Wiley Interdisciplinary Reviews-RNA (2013) 4: 709-722
  11. MORAWIEC E., WICHTOWSKA D., GRACZYK D., CONESA C., LEFEBVRE O., BOGUTA M. Maf1, repressor of tRNA transcription, is involved in the control of gluconeogenetic genes in Saccharomyces cerevisiae. Gene (2013) 526: 16-22
  12. BOGUTA M. Maf1, a general negative regulator of RNA polymerase III in yeast. Biochimica et Biophysica Acta-Gene Regulatory Mechanisms (2013) 1829: 376-384
  13. TUROWSKI T., KARKUSIEWICZ I., KOWAL J., BOGUTA M. Maf1-mediated repression of RNA polymerase III transcription inhibits tRNA degradation via RTD pathway. RNA Journal (2012): 1823-1832  

 Genetic regulation of metabolism in the yeast Saccharomyces cerevisiae

Group leader: dr hab. Róża Kucharczyk 

Staff: Dr Chiranjit Panja (Post-doc), dr Katarzyna Niedźwiecka (Post-doc), mgr Emilia Baranowska (PhD student), mgr Sylwia Pilch (PhD student), mgr. Soroosh Manon (PhD student), Izabela Chojnacka (master student), Aleksandra Wójcicka (bachelor student) 

Research scope 

Mitochondrial ATP synthase biogenesis, regulation and deficiencies: 1. S. cerevisiae as a model organism to study the effects of mutations in mitochondrial ATP6 and ATP8 genes; 2. control of expression of mitochondrially encoded subunits of ATP synthase; 3. biological role of Fmp40 - the only known yeast ampylase.


Research description

ATP synthase is the enzyme of inner mitochondrial membrane responsible for ATP synthesis in the process of oxidative phosphorylation. ATP synthase consists of seventeen structural subunits. Three subunits in yeasts: a, 8 and c (two in human: 8 and a) are encoded by mitochondrial DNA (mtDNA). The biogenesis of this enzyme is a sophisticated process requiring the coordination of gene expression in both nuclear and mitochondrial genomes with the assembly of the enzyme. Activity of the enzyme is closely related to the activity of respiratory chain and controlled, for example by natural hydrolytic activity inhibitor peptide - IF1. A high number of modifications have been identified in the various subunits of ATP synthase, including phosphorylation, acetylation, trimethylation, nitration, S-nitrosylation, and tryptophan oxidation. Some modifications were reported to affect the ATP synthase enzymatic activity, however, in most cases, it remains completely unknown what are the signaling pathways responsible for these modifications, in which tissues or biological conditions these modifications occur, how they impact on the biochemical activity of the target protein and of the holoenzyme. Mutations in genes encoding ATP synthase subunits or assembly factors lead to neurodegenerative diseases, untreatable at the moment.


Our research is divided into several interconnected axes:


1) The mitochondrial ATP synthase is made of subunits of dual genetic origin, nuclear and mitochondrial. We are investigating the mechanisms controlling the biogenesis of ATP synthase: expression of its mitochondrially encoded subunits and their assembly to the enzyme. We are looking for the new proteins involved in these processes. 


2) Cells adapt the energy supply to their demand and deficit in energy production lead to metabolic diseases such as mitochondrial diseases as well as diabetes, heart failure, cancer or neurodegenerative diseases. Our research aims to identify the molecular mechanisms of ATP synthase deficiencies caused by mutations in mitochondrial ATP6 and ATP8 genes, encoding ATP synthase subunits a and 8, in yeast model organism. We have created the yeast strains bearing ten (out of 48) mutations in ATP6 gene leading to neurodegenerative disorders and deciphered their pathogenic mechanism (for four mutations at the molecular level). We continue the work including also mutations in ATP8 gene. We study also the cellular compensatory responses, such as the activation of mitochondrial biogenesis induced by two compounds with the therapeutic potential, and we search for more such a molecules capable stimulate mitochondria. 


3) We have discovered that the human selenoprotein O (SelO) and its yeast (Fmp40) and E. coli (YdiU) homologues, classified by our collaborator to the pseudokinases, have activity of AMPylase. They attach the AMP to the threonine, tyrosine or serine residues in the protein substrates. One of biological role of these proteins is regulation of protein S-glutathionylation levels by AMPylation of the grx family and other proteins during oxidative stress. This is the only AMPylase described in yeast to date and second in human cells. We continue the research aiming to find other than glutaredoxins Fmp40 substrates and understanding the role of this protein in the regulation of mitochondrial bioenergetics.

4) A growing number of proteins studied in yeast display a dual cytosolic and mitochondrial localization. In the goal to screen such mitochondrial proteins we have explored a split-GFP method designed by Cabantous and co-workers in such a way that the localization of one of the two fragments of this Split-GFP would be restricted to the mitochondrial compartment. Split-GFP is based on the partition of the 11 beta (β) strands-composed GFP into one long fragment encompassing the 10 first β strands (β1-10), and one smaller fragment made of the remaining beta strand (β11). We engineered a yeast strain harboring the gene encoding β1-10 fragment of the Split-GFP in the mitochondrial genome, thus translated inside the mitochondrial matrix, while the second β11 Split-GFP fragment can be fused to any nuclear-encoded protein that will be translated by the cytosolic translation machinery. We will engineer a yeast strain/s for studying the inter membrane space localized proteins, expressing β1-10 from mitochondrial DNA attached to the IMS face of IM. 

Expertise & Techniques

Molecular biology (PCR, qRT_PCR, DNA cloning and sequencing, site-directed mutagenesis, also of mitochondrial DNA, etc.)

Yeast genetics (nuclear and mitochondrial genomes), genetic transformation of mitochondria (Biolistics)

Drug screening (in collaboration with JP di RAgo)

Bioenergetic characterization of isolated mitochondria and whole cells (oxygraphy: Clark electrode, spectrofluorometry, enzymatic activities)

Mitochondrial morphology and ultrastructure analysis 

Protein electrophoresis (BN/CN-PAGE, SDS-PAGE) and analysis (staining, activities, Western Blot)

Protein purification (immunoprecipitation, affinity chromatography, tags (His, HA, FLAG))


Key and active collaborations

prof. J-P. di Rago, Institute of Biochemistry and Cell Genetics, CNRS, Bordeaux, (France); 

prof. Hubert Becker,  Strasburg University (France); 

prof. Thomas Meyer, Imperial College London, UK;

prof. Christos Chinopoulos, Semmelweis University, Budapest (Hungary)

prof. Paolo Bernardi, University o Padova (Italy); 

prof. Vincent Tagliabracci, UT Southwestern Medical Center (USA);

prof. Małgorzata Łobocka (IBB PAS, Poland)

prof. Krzysztof Pawłowski, Warsaw University of Life Science (Poland).



2019-2023 “Regulation of cell death and OXPHOS activity by Fmp40 AMPylase in yeast S. cerevisiae”. NCN project nr UMO-2018/31/B/NZ3/01117

2017-2020  „Understanding of the functioning of the mitochondrial ATP synthase by studying in yeast the phenotype of human pathology related mutations in the mitochondrial DNA”, NCN project nr UMO-2016/23/B/NZ3/02098  


Selected publications:

  1. Kucharczyk R, Dautant A, Gombeau K, Godard F, Tribouillard-Tanvier D, di Rago JP. (2019) The pathogenic MT-ATP6 m.8851T>C mutation prevents proton movements within the n-side hydrophilic cleft of the membrane domain of ATP synthase. Biochim Biophys Acta Bioenerg. 1860(7):562-57. 
  2. Kucharczyk R, Dautant A, Godard F, Tribouillard-Tanvier D, di Rago JP. Functional investigation of an universally conserved leucine residue in subunit a of ATP synthase targeted by the pathogenic m.9176 T>G mutation. Biochim Biophys Acta Bioenerg. 2019; 1860(1):52-59, PMID: 30414414
  3. Carraro M, Checchetto V, Sartori G, Kucharczyk R, di Rago JP, Minervini G, Franchin C, Arrigoni G, Giorgio V, Petronilli V, Tosatto SCE, Lippe G, Szabó I, Bernardi P. High-Conductance Channel Formation in Yeast Mitochondria is Mediated by F-ATP Synthase e and g Subunits. Cell Physiol Biochem. 2018; 50(5):1840-1855, PMID: 30423558
  4. Sreelatha A, Yee SS, Lopez VA, Park BC, Kinch LN, Pilch S, Servage KA, Zhang J, Jiou J, Karasiewicz-Urbańska M, Łobocka M, Grishin NV, Orth K, Kucharczyk R, Pawłowski K, Tomchick DR, Tagliabracci VS. Protein AMPylation by an Evolutionarily Conserved Pseudokinase. Cell. 2018; 175(3):809-821.e19, PMID: 30270044
  5. de Taffin de Tilques M, Lasserre JP, Godard F, Sardin E, Bouhier M, Le Guedard M, Kucharczyk R, Petit PX, Testet E, di Rago JP, Tribouillard-Tanvier D. Decreasing cytosolic translation is beneficial to yeast and human Tafazzin-deficient cells. Microb Cell. 2018; 5(5):220-232. PMID: 29796387
  6. Skoczeń N, Dautant A, Binko K, Godard F, Bouhier M, Su X, Lasserre JP, Giraud MF, Tribouillard-Tanvier D, Chen H, di Rago JP, Kucharczyk R. Molecular basis of diseases caused by the mtDNA mutation m.8969G>A in the subunit a of ATP synthase. BBA-BIO 2018; 1859(8):602-611. PMID: 29778688
  7. Klim J, Gładki A, Kucharczyk R, Zielenkiewicz U, Kaczanowski S. Ancestral State Reconstruction of the Apoptosis Machinery in the Common Ancestor of Eukaryotes. G3 (Bethesda). 2018; 8(6):2121-2134. PMID: 2970378
  8. Dautant A, Meier T, Hahn A, Tribouillard-Tanvier D, di Rago JP, Kucharczyk R. ATP Synthase Diseases of Mitochondrial Genetic Origin. Front Physiol. 2018; 9:329. Review. PMID: 2967054
  9. Chen E, Kiebish MA, McDaniel J, Niedzwiecka K, Kucharczyk R, Ravasz D, Gao F, Narain NR, Sarangarajan R, Seyfried TN, Adam-Vizi V, Chinopoulos C. Perturbation of the yeast mitochondrial lipidome and associated membrane proteins following heterologous expression of Artemia-ANT. Sci Rep. 2018; 8(1):5915. PMID: 29651047
  10. Niedzwiecka K, Tisi R, Penna S, Lichocka M, Plochocka D, Kucharczyk R. Two mutations in mitochondrial ATP6 gene of ATP synthase, related to human cancer, affect ROS, calcium homeostasis and mitochondrial permeability transition in yeast. Biochim Biophys Acta Mol Cell Res. 2018; 1865(1):117-131. PMID: 28986220
  11. Wen S, Niedzwiecka K, Zhao W, Xu S, Liang S, Zhu X, Xie H, Tribouillard-Tanvier D, Giraud MF, Zeng C, Dautant A, Kucharczyk R, Liu Z, di Rago JP, Chen H. Identification of G8969>A in mitochondrial ATP6 gene that severely compromises ATP synthase function in a patient with IgA nephropathy.  Sci Rep. 2016; 6:36313. PMID: 27812026 
  12. Żurawik TM, Pomorski A, Belczyk-Ciesielska A, Goch G, Niedźwiedzka K, Kucharczyk R, Krężel A, Bal W. Revisiting Mitochondrial pH with an Improved Algorithm for Calibration of the Ratiometric 5(6)-carboxy-SNARF-1 Probe Reveals Anticooperative Reaction with H+ Ions and Warrants Further Studies of Organellar pH. PLoS One. 2016; 11(8):e0161353. PMID: 27557123
  13. Niedzwiecka K, Kabala AM, Lasserre JP, Tribouillard-Tanvier D, Golik P, Dautant A, di Rago JP, Kucharczyk R Yeast models of mutations in the mitochondrial ATP6 gene found in human cancer cells.  Mitochondrion. 2016;29:7-17. PMID: 27083309
  14.  Lasserre JP, Dautant A, Aiyar RS, Kucharczyk R, Glatigny A, Tribouillard-Tanvier D, Rytka J, Blondel M, Skoczen N, Reynier P, Pitayu L, Rötig A, Delahodde A, Steinmetz LM, Dujardin G, Procaccio V, di Rago JP. Yeast as a system for modeling mitochondrial disease mechanisms and discovering therapies. Dis Model Mech. 2015; 8(6):509-26. Review. PMID: 26035862
  15. Aiyar RS, Bohnert M, Duvezin-Caubet S, Voisset C, Gagneur J, Fritsch ES, Couplan E, von der Malsburg K, Funaya C, Soubigou F, Courtin F, Suresh S, Kucharczyk R, Evrard J, Antony C, St Onge RP, Blondel M, di Rago JP, van der Laan M, Steinmetz LM. Mitochondrial protein sorting as a therapeutic target for ATP synthase disorders. Nat Commun. 2014 Dec 18;5:5585 PMID: 25519239
  16. Kabala AM, Lasserre JP, Ackerman SH, di Rago JP, Kucharczyk R. Defining the impact on yeast ATP synthase of two pathogenic human mitochondrial DNA mutations, T9185C and T9191C. Biochimie. 2014; 100:200-6. PMID: 24316278

Genetic control of sulfur metabolism in fungi

Group leader: Prof. Andrzej Paszewski
Staff: Dr. Jerzy Brzywczy, Dr. Marzena Sieńko


Fungi are able to assimilate inorganic sulfur for synthesis of cysteine and methionine. These are constituents of proteins and serve as precursors for synthesis of other sulfur-containing organic compounds. Our research concentrates on the filamentous fungus Aspergillus nidulans which is one of main fungal models in molecular and genetic studies. The investigations are focus on regulation of alternative pathways of sulfur amino acid synthesis which are under control of at least two systems: sulfur metabolite repression (SMR) which shuts off sulfate assimilation pathway under cysteine sufficiency, and, co called “homocysteine regulon” controlling genes encoding enzymes metabolizing homocysteine (it is toxic when in excess). We have identified the metR gene, encoding a transcription factor specific for some sulfur metabolism-related genes, and the scon genes encoding subunits of SCF ubiquitin lyase which inactivates MetR protein under surplus of cysteine. The investigations involve also a paralog of MetR encoded by the metZ gene. A proteomic and transcriptopmic analysis of sulfur regulatory mutants has been recently lunched to learn how an excess or a shortage of sulfur amino acids influences protein and transcript profile of the cell.

Research grants:

2009-2012 "Changes in proteomic and transcriptomic profile in regulatory mutants of Aspergillus nidulans
                   as a consequence of a shortage or an excess of sulfur compounds", (Ministry of Science and Higher Education)


Selected publications:

  1. Sieńko M., Natorff R., Owczarek S., Olewicki I., Paszewski A. Aspergillus nidulans genes encoding reverse transsufuration enzymes  belong to homocysteine regulon. Curr. Genetics (2009) 55: 561-570
  2. Piłsyk S., Paszewski A. The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion. Curr. Genetics (2009) 55 :301-309
  3. Wortman J.R. (and many authors including S. Piłsyk, A. Paszewski) The 2008 update of Aspergillus nidulans genome annotation: A community effort. Fungal Genetics and Biology (2009) 46: S2 – S13
  4. Wróbel M., Lewandowska I., Bronowicka-Adamska P., Paszewski A. The level of sulfane sulfur in the fungus Aspergillus nidulans wild type and mutant strains. Amino Acids (2009) 37: 565-571


Mechanisms of protein transport in Saccharomyces cerevisiae

Group leader: Prof. Teresa Zoladek

1. Department

Department of Genetics. Genetics and molecular biology of fungi. Mechanisms of protein transport in yeast Saccharomyces cerevisiae

2. Research scope

Mechanisms of protein transport between organelles and plasma membrane, and roles of the actin cytoskeleton and lipids in this transport. Structure of membrane contacts sites and their function in transport of lipids, metal ions and in signalling. The role of Vps13 family proteins, involved in neurodegenerative diseases, in these processes.

3. Research description

Vps13 proteins play a prominent role in human health and disease, yet their precise functions remain obscure. The rare human disorder chorea-acanthocytosis (ChAc) is caused by mutations in hVPS13A gene. The hVps13A protein interacts with actin and regulates the level of phosphatidylinositol 4-phosphate (PI4P) in membranes of neuronal cells. Yeast Vps13 is involved in vacuolar protein transport and, like hVps13A, participates in PI4P metabolism (Fig.1). Vps13 proteins are conserved in eukaryotes (Fig.2). One of the mutations found in ChAc patient causes substitution of amino acid residue I2771R which affects the localization of hVps13A in skeletal muscles. To dissect the mechanism of pathogenesis of I2771R, we created and analyzed a yeast strain carrying the equivalent mutation. We show that in yeast, substitution I2749R causes dysfunction of Vps13 protein in endocytosis and vacuolar transport, although the level of the protein is not affected, suggesting loss of function. We also show that Vps13, like hVps13A, influences actin cytoskeleton organization and binds actin in immunoprecipitation experiments. Vps13-I2749R binds actin, but does not function in the actin cytoskeleton organization. Moreover, we show that Vps13 binds phospholipids, especially phosphatidylinositol 3-phosphate (PI3P), via its SHR_BD and APT1 domains (Fig.2). Substitution I2749R attenuates this ability. Finally, the localization of Vps13-GFP is altered when cellular levels of PI3P are decreased indicating its trafficking within the endosomal membrane system. These results suggest that PI3P regulates the functioning of Vps13, both in protein trafficking and actin cytoskeleton organization. Attenuation of PI3P-binding ability in the mutant hVps13A protein may be one of the reasons for its mislocalization and disrupted function in cells of patients suffering from ChAc (Rzepnikowska et al., 2017, Hum Mol Genet 26(8):1497-1510. doi: 10.1093/hmg/ddx054)


Figure 1. Localization and involvement of Vps13 in various processes in yeast cells. The intracellular sites of Vps13-GFP localization are schematically shown in tones of green and the relevance of Vps13 in particular processes is indicated. Abbreviations for intracellular junctions: NVJ, ER-derived nuclear envelope-vacuole junctions; vCLAMP, vacuole and mitochondria patch; EMJ, endosome–mitochondria junctions; ERMES, endoplasmic reticulum mitochondria encounter structure. Components of a cell: CW, cell wall; EE, early endosome; ER, endoplasmic reticulum; LE, late endosome; Mito, mitochondrion; PM, plasma membrane (Rzepnikowska W. et al., Traffic 18:711-719. doi: 10.1111/tra.12523, modified).


Figure 2. Structure of both, yeast Vps13 and human Vps13A proteins.

A schematic representation of the domain architecture of Vps13 proteins based on Pfam database records and analysis performed using the Phyre2 software. The regions of yeast Vps13 with the ability to bind to lipids in vitro are marked as horizontal bars with associated lipids listed: LPA, lysophosphatidic acid; PA, phosphatidic acid; PI, phosphatidylinositol; PIPs, phosphorylated PI derivatives; PI3P, PI3 phosphate; PI4P, PI4 phosphate; PI5P, PI5 phosphate; PI(3,5)P2, PI(3,5) bisphosphate; PI(4,5)P2, PI(4,5) bisphosphate; PS, phosphatidylserine. Explanation of the domain names in order of their appearance in the protein: Chorein_N, N-terminal region of Chorein (Vps13A); Vps13, Vacuolar sorting-associated protein 13 (Vps13) N-terminal domain (PF16908); VPS13_mid_rpt, repeating region of Vps13 (PF16910); SHR_BD (previously called DUF1162), SHR (SHORT-ROOT transcription factor)-binding domain (PF06650); APT1, domain of maize (Zea mays) aberrant pollen transmission 1 (APT1) protein (PF10351); ATG_C, autophagy-related protein C-terminal domain (PF09333); PH, pleckstrin homology domain (PF00169). (Rzepnikowska et al., 2017, Traffic 18:711-719. doi: 10.1111/tra.12523, modified).


4. Lab members (it is possible to include photographs)

Dr hab. Joanna Kaminska

Mgr Piotr Soczewka, PhD student

Mgr Damian Kolakowski, PhD student

Mgr Patrycja Wardaszka, PhD student


5. Publications and patents

1. Rzepnikowska W, Kaminska J, Kabzińska D, Kochański A. (2020) Pathogenic Effect of GDAP1 Gene Mutations in a Yeast Model. Genes (Basel). 2020 Mar 14;11(3). pii: E310. doi: 10.3390/genes11030310.

2. Soczewka P, Kolakowski D, Smaczynska-de Rooij I, Rzepnikowska W, Ayscough KR, Kaminska J, Zoladek T. (2019) Yeast-model-based study identified myosin- and calcium-dependent calmodulin signalling as a potential target for drug intervention in chorea-acanthocytosis. Dis Model Mech. Jan 28;12(1). pii: dmm036830. doi: 10.1242/dmm.036830.

3. Kaminska J, Kolakowski D. (2018) Białka z rodziny Vps13: od funkcji molekularnej do patogenezy chorób neurodegeneracyjnych. Postępy Biochemii 64(4): 

4. Rzepnikowska W, Flis K, Muñoz-Braceras S, Menezes R, Escalante R, Zoladek T. (2017) Yeast and other lower eukaryotic organisms for studies of Vps13 proteins in health and disease. Traffic 18:711-719. doi: 10.1111/tra.12523. Review.

5. Rzepnikowska W, Flis K, Kaminska J, Grynberg M, Urbanek A, Ayscough KR, Zoladek T. (2017) Amino acid substitution equivalent to human chorea-acanthocytosis I2771R in yeast Vps13 protein affects its binding to phosphatidylinositol 3-phosphate. Hum Mol Genet 26(8):1497-1510. doi: 10.1093/hmg/ddx054.

6. Krol K, Jendrysek J, Debski J, Skoneczny M, Kurlandzka A, Kaminska J, Dadlez M, Skoneczna A. (2017) Ribosomal DNA status inferred from DNA cloud assays and mass spectrometry identification of agarose-squeezed proteins interacting with chromatin (ASPIC-MS). Oncotarget 8(15):24988-25004. doi: 10.18632/oncotarget.15332.

7. Kaminska J, Rzepnikowska W, Polak A, Flis K, Soczewka P, Bala K, Sienko M, Grynberg M, Kaliszewski P, Urbanek A, Ayscough K, Zoladek T. (2016) Phosphatidylinositol-3-phosphate regulates response of cells to proteotoxic stress. Int. J. Bioch. Cell Biol. 79:494-504. 

8. Klionsky DJ, Abdelmohsen K,… Zoladek T…. et al., (2016) Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. 12:1-222. 

9. Jastrzebska Z, Kaminska J, Chelstowska A, Domanska A, Rzepnikowska W, Sitkiewicz E, Cholbinski P, Gourlay C, Plochocka D, Zoladek T. (2015) Mimicking the phosphorylation of Rsp5 in PKA site T761 affects its function and cellular localization Eur. J. Cell Biol. 94:576-588. 

10. Chelstowska A, Jastrzebska Z, Kaminska J, Sadurska A, Plochocka D, Rytka J, Zoladek T. (2015) Hem12, an enzyme of heme biosynthesis pathway, is monoubiquitinated by Rsp5 ubiquitin ligase in yeast cells. Acta Biochim. Pol. 62(3):509-15. 

11. Maciejak A., Leszczynska A., Warchol I., Gora M., Kaminska J., Plochocka D., Wysocka-Kapcinska M., Tulacz D., Siedlecka J., Swiezewska E., Sojka M., Danikiewicz W., Odolczyk N., Szkopinska A., Sygitowicz G., Burzynska B. (2013) The effects of statins on the mevalonic acid pathway in recombinant yeast strains expressing human HMG-CoA reductase. BMC Biotechnology 13(1):68. doi: 10.1186/1472-6750-13-68. 

12. Klionsky DJ, Abdalla FC, Abeliovich H… Zoladek T,… et al. (2012) Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8:445-544.

Patent Nr P 385243 “New modified yeast strain Saccharomyces cerevisiae, method of its construction and application” [submitted 2008, accepted 2016].




Genetic analysis of some hereditary human diseases

Group leader: Dr. Beata Burzyńska
Staff: Dr Monika Góra, M.Sc. Agata Maciejak (Ph.D. student), M.Sc. Dorota Tułacz (Ph.D. student)


Major research directions:

  1. Determination of genetic biomarkers (at mRNA and miRNA level) leading to the left ventricular remodeling after acute myocardial infarction (AMI). Our research is carried out using an experimental myocardial infarction model in rat and blood samples taken from patients after AMI. This project will allow the investigation of the genetics factors which lead to heart decompensation in post-infarction patients. We have shown that the evaluation of the expression of RNA isolated from peripheral blood leukocytes allows the identification of genes whose expression is significantly altered in the acute phase of myocardial infarction.
  2. The study of genetic determinants of congenital hemolytic anemia caused by impaired red blood cell enzyme activity, disturbances in membrane proteins and abnormalities in the structure and synthesis of hemoglobin.
  3. Investigation of statin treatment molecular effects on the cell using yeast experimental model. Yeast expression system was constructed and applied to detect the effects of genetic changes and the type of statin used on cell metabolism. Our results show that the presented model might be helpful in the selection of most efficient lipid-lowering drugs, and maybe can even serve to choose the best therapy for a given patient, leading to the best response and minimizing serious side effects. Finally, the system can be useful for examination of DNA sequence variations in the context of statin therapy.

Research projects:

2015- 2018 “Transcriptomic biomarkers for individual risk stratification  in heart failure”

2015-2017 “Evaluation of circulating microRNA expression profiles in the pathogenesis of heart failure after acute myocardial infarction”

2009- 2015 “The system biology in the investigations of the genetic factors of the coronary disease”

2006-2009  “The functional genomics of the model microorganisms in molecular studies of inherited human diseases and in mechanism of pathogenesis”

- “Molecular analysis of haemolytic anaemias”

- “The use of S. cerevisiae in studies of the vascular endothelium function”

2005-2008 “The analysis of mutations in patients with hereditary haemolytic anaemias” 

2003-2006   “Development of expression filters for detection of genetic mutations responsible for deficiency of membrane proteins of red blood cells in patients with congenital spherocytosis or for other less frequently encountered congenital erythrocyte abnormalities”.


Selected publications:

  1. Warchol I, Gora M, Wysocka-Kapcinska M, Komaszylo J, Swiezewska E, Sojka M,Danikiewicz W, Plochocka D, Maciejak A, Tulacz D, Leszczynska A, Kapur S,Burzynska B. Genetic engineering and molecular characterization of yeast strainexpressing hybrid human-yeast squalene synthase as a tool for anti-cholesterol drug assessment. J Appl Microbiol. 2016 Apr;120(4):877-88. 
  2. Sygitowicz G, Maciejak A, Piniewska-Juraszek J, Pawlak M, Góra M, Burzyńska B, Dłużniewski M, Opolski G, Sitkiewicz D. Interindividual variability of atorvastatin treatment influence on the MPO gene expression in patients after acute myocardial infarction. Acta Biochim Pol. 2016;63(1):89-95.
  3. Szpakowicz A, Kiliszek M, Pepinski W, Waszkiewicz E, Franaszczyk M, SkawronskaM, Ploski R, Niemcunowicz-Janica A, Burzynska B, Tulacz D, Maciejak A, KaminskiMJ, Opolski G, Musial WJ, Kaminski KA. The rs12526453 Polymorphism in an Intron of the PHACTR1 Gene and Its Association with 5-Year Mortality of Patients with Myocardial Infarction. PLoS One. 2015 Jun 18;10(6):e0129820. 
  4. Maciejak A, Kiliszek M, Michalak M, Tulacz D, Opolski G, Matlak K, Dobrzycki S, Segiet A, Gora M, Burzynska B. Gene expression profiling reveals potential prognostic biomarkers associated with the progression of heart failure. Genome Med. 2015 Mar 14;7(1):26. 
  5. Tulacz D, Mackiewicz U, Maczewski M, Maciejak A, Gora M, Burzynska B. Transcriptional profiling of left ventricle and peripheral blood mononuclear cells in a rat model of postinfarction heart failure. BMC Med Genomics. 2013 Nov 8;6:49. 
  6. Gora M, Kiliszek M, Burzynska B. Will global transcriptome analysis allow the detection of novel prognostic markers in coronary artery disease and heart failure? Curr Genomics. 2013 Sep;14(6):388-96. 
  7. Maciejak A, Leszczynska A, Warchol I, Gora M, Kaminska J, Plochocka D, Wysocka-Kapcinska M, Tulacz D, Siedlecka J, Swiezewska E, Sojka M, Danikiewicz W,Odolczyk N, Szkopinska A, Sygitowicz G, Burzynska B. The effects of statins on the mevalonic acid pathway in recombinant yeast strains expressing human HMG-CoA reductase. BMC Biotechnol. 2013 Aug 30;13:68. 
  8. Rawa K, Adamowicz-Salach A, Matysiak M, Trzemecka A, Burzynska B. Coexistence of Gilbert syndrome with hereditary haemolytic anaemias. J Clin Pathol. 2012 Jul;65(7):663-5. 
  9. Kiliszek M, Burzynska B, Michalak M, Gora M, Winkler A, Maciejak A, Leszczynska A, Gajda E, Kochanowski J, Opolski G. Altered gene expression pattern in peripheral blood mononuclear cells in patients with acute myocardial infarction. PLoS One. 2012;7(11):e50054. 
  10. Kaczorowska-Hac B, Burzynska B, Plochocka D, Zak-Jasinska K, Rawa K, Adamkiewicz-Drozynska E. The first reported case of G6PD deficiency due to Seoul  mutation in Poland. Ann Hematol. 2014 May;93(5):879-80. 
  11. Wysocka-Kapcinska M, Lutyk-Nadolska J, Kiliszek M, Plochocka D, Maciag M, Leszczynska A, Rytka J and  Burzynska B. Functional expression Wysocka-Kapcinska  of human HMG-CoA reductase in Saccharomyces cerevisiae: a system to analyze normal and mutated versions of the enzyme in the context of statin treatment. J Appl Microbiol 2009; 106(3):895-902. 
  12. Maciag M, Płochocka D, Adamowicz-Salach A, Burzyńska B. Novel beta-spectrin mutations in hereditary spherocytosis associated with decreased levels of mRNA. Br J Haematol 2009; 146(3):326-32.
  13. Maciag M, Adamowicz-Salach A, Siwicka A, Spychalska J, Burzynska B. The use of real-time PCR technique in the detection of novel protein 4.2 gene mutations that coexist with thalassaemia alpha in a single patient. Eur J Haematol 2009; 83(4):373-7.
  14. Pawlowski PH, Burzyńska B, Zielenkiewicz P. Theoretical model of thalassemic erythrocyte shape transformation J Theor Biol. 2008; 7;254(3):575-9. 
  15. Maciag M, Płochocka D, Adamowicz-Salach A, Jackowska T, Mendek-Czajkowska E, Pawelczyk A, Zdebska E, Burzynska B. Diversity of thalassaemia variants in Poland - screening by real-time PCR. Acta Haematol. (Basel) 2008; 120:153-157.
  16. Kiliszek M., Burzynska B., Styczynski G., Maciag M., Rabczenko D., Opolski G. A1166C polymorphism of the angiotensin AT1 receptor (ATIR) gene alters endothelial response to statin treatment. Clin. Chem. Lab. Med. 2007; 45: 839-842.
  17. Pawlowski P.H., Burzynska B., Zielenkiewicz P. Theoretical model of reticulocyte to erythrocyte shape transformation. J. Theor. Biol. 2006; 243: 24-38.

Patents and patent application:

Patent RP Nr 208956 - Method for detection and differentiation of the diseases belonging to the group hemoglobinopathies, especially thalassemias. 

Patent RP Nr 386922 -  Yeast strain for the biological validation of mevalonic acid pathway inhibitors, process for its preparation and use.  

Patent application P 407163 - Transcriptomic biomarkers, method for determination thereof and use of transcriptomic biomarkers for individual risk assessment of developing post-infarction heart failure

PCT/I82015/000141 - Transcriptomic biomarkers, method for determination thereof and use of transcriptomic biomarkers for individual risk assessment of developing post-infarction heart failure



Mechanisms of cell division

Group leader: Anna Kurlandzka PhD, Dr.Sci., Assoc. Prof.
Staff: Piotr Kowalec, PhD


We study chromosome segregation in mitosis and meiosis focusing on sister chromatid cohesion complex. Our principal model organism is yeast Saccharomyces cerevisiae, but some results have been verified also in human cells. In particular, we are investigating the sister chromatid cohesion complex, composed of evolutionarily conserved and essential proteins. We concentrate on the protein Irr1p/Scc3, which is a multifunctional protein regulating cohesion but it is also involved in other processes. The gene encoding Irr1 was identified in our laboratory, and a few of our papers concern this protein. Mutations in IRR1 gene lead to perturbations in chromosome segregation, but they are also accompanied by defects in other cellular processes, such as cell wall organization. We assume that this may be linked to additional role of Irr1, outside chromatin cohesion. Irr1 is present not only in the nucleus, but also in the cytoplasm. In search of non-nuclear functions of Irr1, we identified a new interacting partner – Imi1 protein, localized in cytoplasm. A lack of Imi1 leads to mitochondrial lesions and impaired respiration. The mitochondrial malfunctioning is coupled to disturbed glutathione homeostasis. The nature of Irr1 – Imi1 interaction is currently under investigation. Human homologues of Irr1p – the stromalins STAG1 and STAG2 – were also studied in terms of its possible non nuclear function. We found that STAG1 has a nuclear localization whereas STAG2 shuttles between the nucleus and the cytoplasm and is exported from the nucleus by a Crm1p exportin–depended mechanism.


Research grants:

2014-2016 “Connections between Irr1 protein involved in segregation of nuclear DNA and the newly identified mitochondrial protein Imi1 of Saccharomyces cerevisiae”, (National Science Centre)

2010-2013 "Nuclear import and export signals in human cohesin SA1 and SA2 identified during heterologous expression in Saccharomyces cerevisiae", (Ministry of Science and Higher Education)

2010-2014 "Post synthetic modifications and role of Irr1/Scc3 cohesin in meiosis initiation in  Saccharomyces cerevisiae", (Ministry of Science and Higher Education)


Recent publications:

  1. Kowalec P, Grynberg M, Pająk B, Socha A, Winiarska K, Fronk J, Kurlandzka A (2015) Newly identified protein Imi1 affects mitochondrial integrity and glutathione homeostasis in Saccharomyces cerevisiae. FEMS Yeast Research 15 pii: fov048
  2. Tarnowski LJ, Milewski M, Fronk J, Kurlandzka A (2015) A compound C-terminal nuclear localization signal of human SA2 stromalin. Acta Biochim Pol. 62: 215-9
  3. Cena A, Skoneczny M, Chełstowska A, Kowalec P, Natorff R, Kurlandzka A (2013) Cohesin Irr1/Scc3 is likely to influence transcription in Saccharomyces cerevisiae via interaction with Mediator complex. Acta Biochim Pol. 60: 233-238
  4. Tarnowski LJ, Kowalec P, Milewski M, Jurek M, Plochocka D, Fronk J, Kurlandzka A (2012) Nuclear import and export signals of human cohesins SA1/STAG1 and SA2/STAG2 expressed in Saccharomyces cerevisiae. PLoS One 7: e38740
  5. Cena A, Kozłowska E, Płochocka D, Grynberg M, Ishikawa T, Fronk J, Kurlandzka A (2008). The F658G substitution in Saccharomyces cerevisiae cohesin Irr1/Scc3 is semi-dominant in the diploid and disturbs mitosis, meiosis and the cell cycle. Eur J Cell Biol. 87: 831-844



Functional genomics of eukaryotic cells’ response to environmental stresses

Group leader: dr hab. Marek Skoneczny

Staff: dr Anna Chełstowska, dr Urszula Natkańska, mgr Błażej Kempiński, mgr Łukasz Rymer


Stress is an inevitable phenomenon encountered by all living organisms. Stress may originate from environmental conditions but also be a side-effect of many intracellular processes. This implicates that creating an inventory of different stresses, as well as mechanisms allowing to counteract the effects of stress is crucial to understanding the rules which govern life on Earth.

One of the characteristics of stress, especially one originating from an external environment, is its unpredictability. Therefore, organisms must be prepared for the encounter with stress. On the other hand, maintaining an entire defense system ready to react to any potential stressful condition would be an enormous burden to any organism. It would also result in a diminished ability of a particular species to survive in confrontation with its competitors. In consequence, stress response is a tightly regulated process. In organisms subjected to stressful conditions a profound re-programming of the whole cellular metabolism is observed. This results, among others, in a significant increase in the level of proteins involved in the protection of cells against stress.

Yeast Saccharomyces cerevisiae proved to be an organism perfectly suited to stress response research. This yeast serves as a model organism in numerous basic science studies. Simultaneously, it is an important organism used in the food industry as well as in production of renewable fuel (ethanol). In such industrial processes, yeast cells encounter much more pronounced stresses that those experienced in mild laboratory conditions. For this reason, the knowledge of yeast stress defense mechanisms has also a very practical aspect. 

Despite intensive studies our knowledge about stress response mechanism is still incomplete. One of the mysteries is the occurrence of genes whose expression is highly increased in response to stress, however their knocking out has scarcely pronounced or practically undetectable influence on the cell’s ability to survive in laboratory conditions. The role of such genes, coding for the proteins which can be considered as elements of the "second defense line", remained unknown for a long period of time. The examples of this class of proteins are S. cerevisiae proteins from the DJ-1/ThiJ/PfpI family: Hsp31p, Hsp32p, Hsp33p, Hsp34p. The analysis of the function of these proteins is one of the objectives of our research team.

Chemical redox reactions are one of the sources of endogenous stress, due to the generation of the reactive oxygen species as the by-products. These types of reactions take place in peroxisomes, one of the cellular organelles. Peroxisomal oxidases’ activities, an example of which is S. cerevisiae acyl-CoA oxidase, result in the production of hydrogen peroxide, subsequently decomposed by peroxisomal catalases. Peroxisome biogenesis, and particularly mechanisms of peroxisomal proteins import, is another topic of studies carried out by our team. Two pathways involved in proteins targeting into this organelle are known. These are so-called PTS1 and PTS2 signal routes, which depend on PTS1 or PTS2 sequences recognized by Pex5p or Pex7p receptors, respectively. However, there exist proteins (the above mentioned acyl-CoA oxidase is one of them), which are transported into the peroxisomes’ matrix independently of so-far identified signals. This indicates that a new mechanism of peroxisomal protein import must exist. The identification of this novel targeting mechanism, in which the recognition of a new PTS3 signal is a crucial part, is another research project of our group. 

We are also in the possession of equipment for the whole-genome micro-array analyses. It consists of micro-array scanner Axon GenePix 4000B, a hybridization oven (Agilent) and suitable software. 

The experiments which can be performed by us include, among  others:

- Transcriptome analysis

- Comparative genome hybridization (aCGH) analysis

- Population analysis of the yeast S. cerevisiae whole gene-deletion collection (using molecular bar-code microarrays)

The equipment we posses allows for visualization and analysis of any experiment that involves Cy3 and Cy5 dyes fluorescence measurements (or their equivalents with similar absorption and emission spectrum) on the microscopic slide 25x75 mm with 5µm resolution.


Ongoing projects:

Assignment of the Hsp31p function in S. cerevisiae cells: depiction of its cellular location and detailed analysis of regulatory systems involved in HSP31 response to environmental stresses.

Analysis of genome-wide transcriptional response of S. cerevisiae to stress induced by high ethanol concentration.

Identification of amino acid residues acting as a PTS3 signal in proteins (such as acyl-CoA oxidase or carnitine acetyltransferase) targeted into the peroxisome matrix via the PTS3 route.

Identification of so-far unidentified peroxisomal proteins targeted into peroxisomes via the PTS3 pathway in S. cerevisiae and other organisms.


Research grants: 

2013-2016  Studies on the topogenesis of PTS3 proteins: a novel targeting route to peroxisomes

2011-2015 The function and intracellular localization of Saccharomyces cerevisiae Hsp31p stress response protein; functional implications for its ortholog of Candida albicans.


Selected publications:

  1. Natkańska U, Skoneczna A, Skoneczny M.
    Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III.
    Cell Stress Chaperones. 2017 Dec 20. doi: 10.1007/s12192-017-0868-8. [Epub ahead of print]
  2. Jończyk M, Sobkowiak A, Trzcinska-Danielewicz J, Skoneczny M, Solecka D, Fronk J, Sowiński P.
    Global analysis of gene expression in maize leaves treated with low temperature. II. Combined effect of severe cold
    (8°C) and circadian rhythm.
    Plant Mol Biol. 2017 Oct;95(3):279-302.
  3. Krol K, Jendrysek J, Debski J, Skoneczny M, Kurlandzka A, Kaminska J, Dadlez M, Skoneczna A.
    Ribosomal DNA status inferred from DNA cloud assays and mass spectrometry identification of agarose-squeezed proteins interacting with chromatin (ASPIC-MS).
    Oncotarget. 2017 Apr 11;8(15):24988-25004.
  4. Natkańska U, Skoneczna A, Sieńko M, Skoneczny M.
    The budding yeast orthologue of Parkinson's disease-associated DJ-1 is a multi-stress response protein protecting cells against toxic glycolytic products.
    Biochim Biophys Acta. 2017 Jan;1864(1):39-50.
  5. Dabrowska M, Skoneczny M, Zielinski Z, Rode W.
    Wnt signaling in regulation of biological functions of the nurse cell harboring Trichinella spp.
    Parasit Vectors. 2016 Sep 2;9(1):483.
  6. Adamczyk J, Deregowska A, Skoneczny M, Skoneczna A, Natkanska U, Kwiatkowska A, Rawska E, Potocki L, Kuna E, Panek A, Lewinska A, Wnuk M.
    Copy number variations of genes involved in stress responses reflect the redox state and DNA damage in brewing yeasts.
    Cell Stress Chaperones. 2016 Sep;21(5):849-64.
  7. Adamczyk J, Deregowska A, Skoneczny M, Skoneczna A, Kwiatkowska A, Potocki L, Rawska E, Pabian S, Kaplan J, Lewinska A, Wnuk M.
    Adaptive response to chronic mild ethanol stress involves ROS, sirtuins and changes in chromosome dosage in wine yeasts.
    Oncotarget. 2016 May 24;7(21):29958-76.
  8. Sobkowiak A, Jończyk M, Adamczyk J, Szczepanik J, Solecka D, Kuciara I, Hetmańczyk K, Trzcinska-Danielewicz J, Grzybowski M, Skoneczny M, Fronk J, Sowiński P. (2016)
    Molecular foundations of chilling-tolerance of modern maize.
    BMC Genomics. 17(1):125.
  9. Skoneczna A, Kaniak A, Skoneczny M. (2015)
    Genetic instability in budding and fission yeast-sources and mechanisms.
    FEMS Microbiol Rev.39(6): 917-67.
  10. Krol K, Brózda I, Skoneczny M, Bretner M, Skoneczna A. (2015)
    A genomic screen revealing the importance of vesicular trafficking pathways in genome maintenance and protection against genotoxic stress in diploid Saccharomyces cerevisiae cells.
    PLOS One. 10(3): e0120702.
  11. Deregowska A, Adamczyk J, Kwiatkowska A, Gurgul A, Skoneczny M, Skoneczna A, Szmatola T, Jasielczuk I, Magda M, Rawska E, Pabian S, Panek A, Kaplan J, Lewinska A, Wnuk M. (2015)
    Shifts in rDNA levels act as a genome buffer promoting chromosome homeostasis.
    Cell Cycle. 14(21): 3475-87
  12. Deregowska A, Skoneczny M, Adamczyk J, Kwiatkowska A, Rawska E, Skoneczna A, Lewinska A, Wnuk M. (2015)
    Genome-wide array- CGH analysis reveals YRF1 gene copy number variation that modulates genetic stability in distillery yeasts.
    Oncotarget. 6(31): 30650-63.
  13. Piłsyk S, Natorff R, Sieńko M, Skoneczny M, Paszewski A, Brzywczy J. (2015)
    The Aspergillus nidulans metZ gene encodes a transcription factor involved in regulation of sulfur metabolism in this fungus and other Eurotiales.
    Curr Genet. 61(2):115-25.
  14. Sieńko M, Natorff R, Skoneczny M, Kruszewska J, Paszewski A, Brzywczy J. (2014)
    Regulatory mutations affecting sulfur metabolism induce environmental stress response in Aspergillus nidulans.
    Fungal Genet Biol. 65:37-47.
  15. Moniuszko G, Skoneczny M, Zientara-Rytter K, Wawrzyńska A, Głów D, Cristescu SM, Harren FJ, Sirko A. (2013)
    Tobacco LSU-like protein couples sulphur-deficiency response with ethylene signalling pathway.
    J Exp Bot.64(16):5173-82.
  16. Cena A, Skoneczny M, Chełstowska A, Kowalec P, Natorff R, Kurlandzka A. (2013)
    Cohesin Irr1/Scc3 is likely to influence transcription in Saccharomyces cerevisiae via interaction with Mediator complex.
    Acta Biochim Pol.;60(2):233-8.
  17. Dabrowska M, Skoneczny M, Rode W. (2011)
    Functional gene expression profile underlying methotrexate-induced senescence in human colon cancer cells.
    Tumour Biol. 32(5):965-76.
  18. Alabrudzińska M, Skoneczny M, Skoneczna A. (2011)
    Diploid-specific genome stability genes of S. cerevisiae: Genomic screen reveals haploidization as an escape from persisting DNA rearrangement stress.
    PLOS One 6(6): e21124.
  19. Dabrowska M, Skoneczny M, Zielinski Z, Rode W. (2008)
    Nurse cell of Trichinella spp. as a model of long-term cell cycle arrest.
    Cell Cycle. 7(14):2167-78.
  20. Skoneczna A, McIntyre J, Skoneczny M, Policińska Z, Śledziewska-Gójska E. (2007)
    Polymerase eta is a short-lived, proteasomally degraded protein that is temporarily stabilized following UV irradiation in Saccharomyces cerevisiae.
    J. Mol. Biol. 366: 1074-1086.
  21. Skoneczna A, Miciałkiewicz A, Skoneczny M. (2007)
    Saccharomyces cerevisiae Hsp31p, a stress response protein conferring protection against reactive oxygen species.
    Free Radic. Biol. Med. 42: 1409-1420.