Department of Molecular Biology: Zylicz Laboratory

Maciej Żylicz



Maciej Żylicz,
PhD, Professor




1992 Professor, nomination by the President of the Republic of Poland
1986 DSc Habil in Molecular Biology, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland
1980 PhD in Biochemistry, Medical University of Gdansk, Poland
1977 MSc in Physics, University of Gdansk, Poland (student of physics and biology

Post-doctoral Training:
1982-1984 Department of Cellular, Viral and Molecular Biology, University of Utah, Salt Lake City, Utah, USA, and Department of Biochemistry, Stanford University, Stanford, California, USA
1979-1981 Department of Biochemistry, University of Gdansk, Poland

Professional Employment:
2005-Present President, Executive Director, Foundation for Polish Science
1999-Present Head, Department of Molecular Biology, IIMCB
1994-1999 Head, Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, Poland
1991-1994 Head, Department of Molecular Biology, University of Gdansk, Poland
1993-1994 Visiting Professor, University of Utah, Medical Center, Institute of Oncology, Salt Lake City, Utah, USA
1990-1993 Vice President, University of Gdansk, Poland
1988-1991 Associate Professor, Department of Molecular Biology, University of Gdansk, Poland
1981-1988 Assistant Professor, Department of Biochemistry, University of Gdansk, Poland

Other Professional Activities:
2010-2015 Advisor of the President of the Republic of Poland
2010-2014 Member, ERC Identifi cation Committee (appointed by European Commission)
2010-2014 Chair of Selection Committee, Council of the National Science Center, Poland
2008-2010 Panel Chair, Molecular and Structural Biology and Biochemistry (LS1), ERC
2000-2004 Chair of Biology, Earth Sciences and Environmental Protection Commission, State Committee for Scientific Research, Poland
2000-2001 Chair of Basic Science Commission, State Committee for Scientifi c Research, Poland

Membership in Scientific Societies, Organizations, and Panels:
• European Molecular Biology Organization (EMBO), Member
• Polish Academy of Sciences, Full Member
• German National Academy of Sciences Leopoldina, Member
• Polish Academy of Arts and Sciences, Member
• Academia Europaea, Member
• European Academy of Cancer Research, Member
• American Society of Biochemistry and Molecular Biology, Member
• Advisory Editorial Board, EMBO Journal, EMBO Reports (2004-2008), and IUBMB Life, Member
• EMBO Council (2004-2007), Member
• Selection Committee, EMBO Young Investigator Programme (2001-2003), Member
• European Molecular Biology Conference (2001-2004), Polish delegate
• European Science Foundation Life Science Committee (2003-2005), Polish Delegate
• Selection Committee, Special DFG Programmes (2001-2005), Member
• Max Planck Society, Member of Senate (2012-Present)
• State Committee for Scientifi c Research (1997-2004), Member

Honors, Prizes, Awards:
2015 Commandor's Cross of the Order of Polonia Restituta
2013 Doctor Honoris Causa, Jagiellonian University
2011 Doctor Honoris Causa, University of Gdansk
2008 Offi cer’s Cross of the Order of Polonia Restituta (awarded by the President of the Republic of Poland)
2007 Doctor Honoris Causa, University of Wrocław
2002 Prime Minister Award for Scientifi c Achievements
2001 Marchlewski Award, Committee of Biochemistry and Biophysics, Polish Academy of Sciences
1999 Award in biological/medical sciences, Foundation for Polish Science
1996, 2007, 2010 Awards for best biochemistry work performed in Polish laboratories, Polish Biochemical Society
1994 Award from Ministry of Education
1993 Heweliusz Prize for Scientific Achievements (awarded by President of Gdansk)
1990 Award from Polish Academy of Sciences
1986 Individual Award for Scientific Achievements, Polish Academy of Sciences

Liberek K, Skowyra D, Osipiuk J, Banecki B, Wojtkowiak D, Jakóbkiewicz J, Puzewicz J, Barski P, King F, Bućko-Justyna M, Kudła G, Helwak A, Lipiński L, Szymańska Z, Urbański J

Habilitations DSc Performed in Department:
K. Liberek, W. Werel, J. Marszałek , I. Konieczny , A. Wawrzynow , B. Banecki , P. Bieganowski.

Professor Titles Received:
K. Liberek, J. Marszałek, I. Konieczny, A. Wawrzynow.

Over 80 publications in primary scientifi c journals, including two papers published in Cell, six in EMBO J, six in Proc Natl Acad Sci USA, and more than 30 in J Biol Chem. These papers were cited more than 6200 times (including 23 papers cited more than 100 times)

Maciej Zylicz- past scientific accomplishments:
1. Isolation of the first Hsp70, the bacterial dnaK gene product, and discovery that Hsp70 possesses a weak ATPase activity that is stimulated by protein substrate (Zylicz et al., 1983, 249 citations). Subsequently, stimulation of Hsp70 ATPase activity in the presence of different protein and peptide substrates was demonstrated for all tested procaryotic and eucaryotic Hsp70s.
2. Isolation of the first Hsp40, the bacterial dnaJ gene product. Zylicz et al., 1985, 162 citations)
3. Isolation of the GrpE protein co-chaperone (Zylicz et al., 1986, 154 citations)
4. Role of DnaK and DnaJ heat shock proteins in the initiation of lambda DNA replication (Liberek et al., 1988-179 citations).
5. DnaK/DnaJ/GrpE chaperone machine dissociates the aggregated RNA Polymerase in an ATP-dependent reaction (Skowyra et al., 1990;-356 citations, Ziemienowicz et al., 1993,107 citations). Subsequently, the ability of Hsp70 chaperone machine to stimulate the dissociation of protein aggregates or more structured protein oligomers was demonstrated for all tested procaryotic and eucaryotic Hsp70s.
6. Reconstitution in vitro of the bacteriophage lambda DNA replication system (Zylicz et al., 1989, 247citations). For years this assay was utilized as a functional assay for purification of co-chaperones DnaJ and GrpE.
7. Purified bacterial DnaJ and GrpE protein efficiently stimulate DnaK ATPase activity (Liberek et al., 1991, 654 citations). DnaJ protein in this reaction accelerates the rate of ATP hydrolysis, whereas GrpE is a nucleotide exchange factor that stimulates the release of ADP from DnaK. Recently it was shown that functional interaction between DnaK and DnaJ is a paradigm for all tested procaryotic and eucaryotic systems.
8. Hsp40 and ATP hydrolysis activate Hsp70 for binding to different substrates (Wawrzynow et al., 1995, 199 citations). Similar mechanisms have also been observed for eucaryotic Hsc70 and Hsp40 (Misselwitz et al., 1998).
9. Discovery of a new subunit of AAA protease: ClpX (Wojtkowiak et al., 1994, 199 citations)
10. ATPase subunit of Clp protease possesses a chaperone activity (Wawrzynow et al., 1995, 200 citations). Similar results were independently obtained by two other laboratories (S. Lindquist and S. Wickner).
11. Discovery that wild type p53 tumor suppressor protein requires molecular chaperones for its antitumor activity (Zylicz et al., 2001, 143 citations; King et al., 2001, 104 citations; Walerych et al. 2004, 77 citations, Walerych et al., 2009, 24 citations)
12. Discovery that MDM2 oncogene possesses a molecular chaperone activity (Wawrzynow et. al., 2007, 33 citations)

Selected publications since 2001:
• Wiech M., Olszewski M.B., TraczGaszewska Z., Wawrzynow B., Zylicz M., Zylicz A. (2012) Molecular Mechanism of Mutant p53 Stabilization: The Role of HSP70 and MDM2, PLOS ONE 7(12) e51426

• Walerych D, Gutkowska M, Klejman MP, Wawrzynow B, Tracz Z, Wiech M, Zylicz M, Zylicz A. (2010) ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein. J Biol Chem 285, 32020-32028

• Zubrienė A, Gutkowska M, Matulienė J, Chaleckis R, Michailovienė V, Voroncova A, Venclovas C, Zylicz A, Zylicz M, Matulis D. (2010) Thermodynamics of radicicol binding to human Hsp90 alpha and beta isoforms. Biophys Chem, 152, 153-163

• Walerych D., Olszewski M., Gutkowska M., Helwak A., Zylicz M., Zylicz A., (2009) Hsp70 molecular chaperones are required to support p53 tumour suppressor activity under stress conditions. Oncogene 28, 4284-4294

• Narayan V, Eckert M, Zylicz A, Zylicz M, Ball LK. (2009) Cooperative regulation of the IRF-1 tumour suppressor protein by core components of the molecular chaperone machinery. J Biol Chem, 284- 25889-99

• Szymanska Z, Zylicz M. (2009) Mathematical modeling of heat shock proteins synthesis in response to temprerature change. J Math Biol, 58: 819-844

• Wawrzynow B., Zylicz A., Wallace M., Hupp T., Zylicz M. MDM2 Chaperones the p53 Tumor Suppressor. J Biol Chem. (2007) 282:32603-12

• Kudla G, Lipinski L, Caffin F, Helwak A, Zylicz M (2006) High guanine and cytosine content increases mRNA levels in mammalian cells. PLoS Biol. 4: 0933-42

• Jassem J, Jassem E, Jakobkiewicz-Banecka J, Rzyman W, Badzio A, Dziadziuszko R, Kobierska-Gulinda G, Szymanowska A, Skrzypski M, Zylicz M (2004) P53 and K-ras mutations are frequent events in microscopically negative surgical margins from patients with non-small cell lung carcinoma. Cancer, 100: 1951-1960

• Dworakowska D, Jassem E, Jassem J, Peters B, Dziadziuszko R, Zylicz M, Jakobkiewicz-Banecka J, Kobierska-Gulida G, Szymanowska A, Skokowski J, Roessner A, Schneider-Stock R (2004) MDM2 gene amplification: a new independent factor of adverse prognosis in non-small cell lung cancer (NSCLC). Lung Cancer 43: 285-295

• Walerych D, Kudla G, Gutkowska M, Wawrzynow B, Muller L, King FW, Helwak A, Boros J, Zylicz A, Zylicz M (2004) Hsp90 Chaperones Wild-type p53 Tumor Suppressor Protein. J. Biol. Chem., 279: 48836-48845

• Jassem E, Niklinski J, Rosell R, Niklinska W, Jakobkiewicz J, Monzo M, Chyczewski L, Kobierska G, Skokowski J, Zylicz M, Jassem J (2001) Types and localisation of p53 gene mutations. A report on 332 non-small cell lung cancer patients. Lung Cancer, 34: 47-51

• Zylicz M, Wawrzynow A (2001) Insights into the function of Hsp70 chaperones. IUBMB, 51: 283-287

• King FW, Wawrzynow A, Hohfeld J, Zylicz M (2001) Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. EMBO J. 20: 6297-6305

• Zylicz M, King FW, Wawrzynow A (2001) Hsp70 interactions with the p53 tumour suppressor protein. EMBO J. 20: 4634-4638

• Genevaux P, Wawrzynow A, Zylicz M, Georgopoulos C, Kelley WL (2001) DjlA is a Third DnaK Co-chaperone of Escherichia coli, and Dj1A-mediated Induction of Colanic Acid Capsule Requires Dj1A-DnaK Interaction. J. Biol. Chem. 276: 7906-7912

• Banecki B, Wawrzynow A, Puzewicz J, Georgopoulos C, Zylicz M (2001) Structure–function analysis of the zincbinding region of the ClpX molecular chaperone. J. Biol. Chem. 276: 18843-18848