Michal Zolkiewski

Summary

Affiliation: Kansas State University
Country: USA

Publications

  1. pmc Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis
    Ting Zhang
    Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, United States of America
    PLoS ONE 8:e62454. 2013
  2. pmc Aggregate reactivation mediated by the Hsp100 chaperones
    Michal Zolkiewski
    Department of Biochemistry, Kansas State University, Manhattan, 66506, USA
    Arch Biochem Biophys 520:1-6. 2012
  3. pmc Nucleotide-dependent oligomerization of ClpB from Escherichia coli
    M Zolkiewski
    Department of Biochemistry, Kansas State University, Manhattan 66506, USA
    Protein Sci 8:1899-903. 1999
  4. pmc A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
    Michal Zolkiewski
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Mol Microbiol 61:1094-100. 2006
  5. pmc Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB
    Maria Nagy
    Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
    Protein Sci 18:287-93. 2009
  6. ncbi request reprint Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity
    Zhonghua Liu
    Department of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan 66506, USA
    J Mol Biol 321:111-20. 2002
  7. ncbi request reprint The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    Micheal E Barnett
    Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA
    J Biol Chem 280:34940-5. 2005
  8. pmc Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB
    Vladimir Akoev
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Protein Sci 13:567-74. 2004
  9. pmc Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
    Ting Zhang
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Proteins 80:2758-68. 2012
  10. pmc Domain stability in the AAA+ ATPase ClpB from Escherichia coli
    Maria Nagy
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Arch Biochem Biophys 453:63-9. 2006

Research Grants

  1. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2000
  2. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2001
  3. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2002
  4. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2003
  5. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2005

Collaborators

Detail Information

Publications20

  1. pmc Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis
    Ting 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...
  2. pmc Aggregate reactivation mediated by the Hsp100 chaperones
    Michal Zolkiewski
    Department of Biochemistry, Kansas State University, Manhattan, 66506, USA
    Arch Biochem Biophys 520:1-6. 2012
    ....
  3. pmc Nucleotide-dependent oligomerization of ClpB from Escherichia coli
    M 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...
  4. pmc A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
    Michal Zolkiewski
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Mol Microbiol 61:1094-100. 2006
    ....
  5. pmc Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB
    Maria 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...
  6. ncbi request reprint Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity
    Zhonghua Liu
    Department of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan 66506, USA
    J Mol Biol 321:111-20. 2002
    ....
  7. ncbi request reprint The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    Micheal 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...
  8. pmc Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB
    Vladimir Akoev
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Protein Sci 13:567-74. 2004
    ....
  9. pmc Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
    Ting 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...
  10. pmc Domain stability in the AAA+ ATPase ClpB from Escherichia coli
    Maria Nagy
    Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA
    Arch Biochem Biophys 453:63-9. 2006
    ....
  11. pmc Synergistic cooperation between two ClpB isoforms in aggregate reactivation
    Maria 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...
  12. pmc Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli
    Micheal 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...
  13. doi request reprint Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum
    Fabrice Ngansop
    Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA
    Biochem Biophys Res Commun 439:191-5. 2013
    ..Our results indicate that the chaperone activity of PfClpB1 may support survival of Plasmodium falciparum by maintaining the folding status and activity of apicoplast proteins. ..
  14. pmc Biochemical characterization of Anopheles gambiae SRPN6, a malaria parasite invasion marker in mosquitoes
    Chunju 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...
  15. pmc Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli
    Vekalet Tek
    Department of Biochemistry, 104 Willard Hall, Kansas State University, Manhattan, KS 66506, USA
    Protein Sci 11:1192-8. 2002
    ....
  16. pmc Characterization of human torsinA and its dystonia-associated mutant form
    Zhonghua 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...
  17. pmc Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
    Shannon 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...
  18. ncbi request reprint The N-terminal domain of Escherichia coli ClpB enhances chaperone function
    I 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...
  19. ncbi request reprint Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli
    Sabina Kedzierska
    Department of Biochemistry, University of Gdansk, Gdansk, Poland
    Arch Biochem Biophys 444:61-5. 2005
    ....
  20. pmc Structure and function of the middle domain of ClpB from Escherichia coli
    Sabina 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 Grants5

  1. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2000
    ..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. ..
  2. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2001
    ..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. ..
  3. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2002
    ..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. ..
  4. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal Zolkiewski; Fiscal Year: 2003
    ..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. ..
  5. STRUCTURE AND FUNCTION OF HSP 100 PROTEINS
    Michal 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. ..