Michal Zolkiewski, Ph.D., Professor
Office: 141 Chalmers Hall
B.S., University of Warsaw, Poland
Areas of specialty
- Protein structure and function
- Protein folding, misfolding and aggregation
- AAA+ ATPases in cellular physiology and pathogenesis
- Molecular chaperones
- Development of novel antimicrobials
Nearly every process in a living cell is carried out by protein complexes with highly organized structure and undergoing dynamic transformations. Our research is focused on the AAA+ superfamily of proteins. 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 biological 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.
Ranaweera, C. B., Glaza, P., Yang, T., and Zolkiewski, M.: “Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli”, Arch. Biochem. Biophys., 655, 12-17, 2018.
Kuczynska-Wisnik, D., Cheng, C., Ganta, R. R., and Zolkiewski, M.: ”Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells”, FEMS Microbiol. Lett., 364 (6): fnx059, 2017.
Zhang, T., Kedzierska-Mieszkowska, S., Liu, H., Cheng, C., Ganta, R. R. and Zolkiewski, M.: “Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis”, PLoS ONE 8(5): e62454, 2013.
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.
Zolkiewski, M.: “A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases”, Mol. Microbiol. 61, 1094-1100, 2006.