Research Topics
| Michal ZolkiewskiSummaryAffiliation: Kansas State University Country: USA Publications
Research Grants
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Detail Information
Publications
Aggregate reactivation mediated by the Hsp100 chaperonesMichal Zolkiewski
Department of Biochemistry, Kansas State University, Manhattan, 66506, USA
Arch Biochem Biophys 520:1-6. 2012....
Nucleotide-dependent oligomerization of ClpB from Escherichia coliM Zolkiewski
Department of Biochemistry, Kansas State University, Manhattan 66506, USA
Protein Sci 8:1899-903. 1999..These results indicate that the oligomerization reactions of ClpB are similar to those of other Hsp100 proteins...
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPasesMichal Zolkiewski
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
Mol Microbiol 61:1094-100. 2006....
Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpBMaria Nagy
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
Protein Sci 18:287-93. 2009..We postulate that AAA+ ATPases with the noncanonical Walker A might utilize distinct mechanisms to couple the ATPase cycle with their substrate-remodeling activity...
Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activityZhonghua Liu
Department of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan 66506, USA
J Mol Biol 321:111-20. 2002....
The amino-terminal domain of ClpB supports binding to strongly aggregated proteinsMicheal E Barnett
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
J Biol Chem 280:34940-5. 2005..In summary, we provided evidence for an essential role of the N-terminal domain of ClpB in recognition and binding strongly aggregated proteins...
Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpBVladimir Akoev
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
Protein Sci 13:567-74. 2004....
Domain stability in the AAA+ ATPase ClpB from Escherichia coliMaria Nagy
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
Arch Biochem Biophys 453:63-9. 2006....
Synergistic cooperation between two ClpB isoforms in aggregate reactivationMaria Nagy
Department of Biochemistry, Kansas State University, 141 Chalmers Hall, Manhattan, KS 66506, USA
J Mol Biol 396:697-707. 2010..Our results suggest that the functionality of other AAA+ ATPases may be also optimized by interaction and synergistic cooperation of their isoforms...
Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coliMicheal E Barnett
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
Biochemistry 41:11277-83. 2002..Interestingly, we have identified a conserved residue within the C-terminal domain (Arg819) which does not participate directly in nucleotide binding but is essential for the chaperone activity of ClpB...
Biochemical characterization of Anopheles gambiae SRPN6, a malaria parasite invasion marker in mosquitoesChunju An
Division of Biology, Kansas State University, Manhattan, Kansas, United States of America
PLoS ONE 7:e48689. 2012..Taken together, our results strongly suggest that AgSRPN6 takes on a native serpin fold and is an inhibitor of trypsin-like serine proteinases...
Characterization of human torsinA and its dystonia-associated mutant formZhonghua Liu
Department of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan, KS 66506, USA
Biochem J 374:117-22. 2003..This indicates that the dystonia-associated mutation produces a structurally distinct, possibly misfolded, form of torsinA, which cannot be properly processed in the secretory pathway of eukaryotic cells...
Stability and interactions of the amino-terminal domain of ClpB from Escherichia coliVekalet Tek
Department of Biochemistry, 104 Willard Hall, Kansas State University, Manhattan, KS 66506, USA
Protein Sci 11:1192-8. 2002....
Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensisTing Zhang
Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, United States of America
PLoS ONE 8:e62454. 2013..This study sets the stage for assessing the importance of the chaperone activity of ClpB for E. chaffeensis growth within the mammalian and tick hosts...
Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiencyTing Zhang
Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
Proteins 80:2758-68. 2012..Moreover, our results suggest that selective pressure on the linker sequence may be crucial for maintaining the optimal efficiency of aggregate reactivation by ClpB...
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activityShannon M Doyle
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health NIH, Bethesda, Maryland 20892, USA
Nat Struct Mol Biol 14:114-22. 2007..We suggest that this versatility in reaction mechanism enables ClpB and Hsp104 to reactivate the entire aggregated proteome after stress and enables Hsp104 to control prion inheritance...
The N-terminal domain of Escherichia coli ClpB enhances chaperone functionI Ting Chow
Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA 98195, USA
FEBS Lett 579:4242-8. 2005..Our results are consistent with a model in which the N-domain of ClpB95 maximizes substrate processing under conditions where the cellular supply of free DnaK-DnaJ is limiting...
Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coliSabina Kedzierska
Department of Biochemistry, University of Gdansk, Gdansk, Poland
Arch Biochem Biophys 444:61-5. 2005....
Structure and function of the middle domain of ClpB from Escherichia coliSabina Kedzierska
Department of Biochemistry, University of Gdansk, Gdansk, Poland
Biochemistry 42:14242-8. 2003..The heptad repeats are likely involved in stabilization of an intra-MD helical bundle rather than an intersubunit coiled coil...
Research Grants
- STRUCTURE AND FUNCTION OF HSP 100 PROTEINSMichal Zolkiewski; Fiscal Year: 2005..Characterize interactions between ClpB95 or ClpB80 and the co-chaperones (DnaK, DnaJ, GrpE). 3. Characterize the role of ClpB95 or ClpB80 and the three co-chaperones in the disaggregation and reactivation of luciferase. ..
