Cellular and Molecular Life Sciences CMLS

, Volume 59, Issue 10, pp 1598–1606

The DnaK/ClpB chaperone system from Thermus thermophilus

  • S. Schlee
  • J. Reinstein

DOI: 10.1007/PL00012486

Cite this article as:
Schlee, S. & Reinstein, J. CMLS, Cell. Mol. Life Sci. (2002) 59: 1598. doi:10.1007/PL00012486

Abstract.

Proteins of thermophilic organisms are adapted to remain well structured and functional at elevated temperatures. Nevertheless like their 'cousins' that reside at medium temperatures, they require the assistance of molecular chaperones to fold properly and prevent aggregation. This review compares structural and functional properties of the DnaK/ClpB systems of Thermus thermophilus and, mainly, Escherichia coli (DnakTth and DnakEco). Many elemental properties of these systems remain conserved. However, in addition to a general increase of the thermal stability of its components, the DnakTth system shows profound differences in its regulation, and genetic as well as oligomeric organization. Whether these differences are unique or represent general strategies of adaptation to life at elevated temperatures remains to be clarified.

Key words. Protein folding; chaperone; DnaK; DnaJ; GrpE; ClpB; heat-shock; thermophile.

Copyright information

© Birkhäuser Verlag, 2002

Authors and Affiliations

  • S. Schlee
    • 1
  • J. Reinstein
    • 1
  1. 1.Max-Planck-Institute for Molecular Physiology, Department of Physical Biochemistry, Otto-Hahn-Str. 11, 44227 Dortmund (Germany), Fax: +49 231 133 2699, e-mail: joachim.reinstein@mpi-dortmund.mpg.deDE