Michal Zolkiewski, Ph.D., Associate Professor
Chair Graduate Biochemistry Group
 Contact informationOffice: 176 Chalmers Hall EducationB.S., University of Warsaw, Poland |
Areas of specialty
- Protein structure and function
- Protein folding, misfolding and aggregation
- AAA+ ATPases
- Molecular chaperones
Nearly every process in a living cell is carried out by protein complexes with highly organized structure. Among sophisticated protein machines, the AAA+ superfamily of proteins has recently attracted attention of researchers. AAA stands for "ATPases associated with a variety of cellular activities", which implies that these proteins use energy from ATP and perform a variety of functions. Our laboratory performs basic research oriented towards understanding molecular mechanisms underlying the function of AAA+ proteins. We use a combination of biological, biochemical and biophysical experimental approaches to study interactions between proteins, protein localization inside living cells, and structural changes in proteins and protein complexes.
Selected publications
Zolkiewski, M. and Wu, H.-C.: “Emerging Area: TorsinA, a Novel ATP-Dependent Factor Linked to Dystonia” in Witt, S. N. (ed.), Protein Chaperones and Protection from Neurodegenerative Diseases, Wiley, 2011.
Nagy, M., Guenther, I., Akoyev, V., Barnett, M. E., Zavodszky, M. I., Kedzierska-Mieszkowska, S. and Zolkiewski, M.: “Synergistic cooperation between two ClpB isoforms in aggregate reactivation”, J. Mol. Biol. 396, 697-707, 2010.
Nagy, M., Wu, H.-C., Liu, Z., Kedzierska-Mieszkowska, S. and Zolkiewski, M.: “Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB”, Protein Sci. 18, 287-293, 2009.
Zolkiewski, M.: "ClpB: a chaperone for protein disaggregation", in Houry, W. (ed.), Molecular Chaperones: Principles and Diseases, The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London, 2007.
Doyle, S. M., Shorter, J., Zolkiewski, M., Hoskins, J. R., Lindquist, S. and Wickner, S.: “Asymmetric deceleration of ClpB and Hsp104 ATPase activity unleashes protein-remodeling activity”, Nature Struct. Mol. Biol. 14, 114-122, 2007.
Nagy, M., Akoev, V. and Zolkiewski, M.: “Domain Stability in the AAA+ ATPase ClpB from Escherichia coli”, Arch. Biochem. Biophys. 453, 61-67, 2006.
Zolkiewski, M.: “A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases”, Mol. Microbiol. 61, 1094-1100, 2006.
Barnett, M. E., Nagy, M., Kedzierska, S. and Zolkiewski, M.: “The Amino-Terminal Domain of ClpB Supports Binding to Strongly Aggregated Proteins”, J. Biol. Chem. 280, 34940-34945, 2005.