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Research Article

Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle

C. Ratzke, M. Mickler, B. Hellenkamp, J. Buchner, and T. Hugel
PNAS first published August 24, 2010; https://doi.org/10.1073/pnas.1000916107
C. Ratzke
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M. Mickler
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B. Hellenkamp
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J. Buchner
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T. Hugel
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  • For correspondence: thorsten.hugel@ph.tum.de
  1. Edited by George H. Lorimer, University of Maryland, College Park, MD, and approved July 22, 2010 (received for review January 26, 2010)

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Abstract

The molecular chaperone heat shock protein 90 (Hsp90) is an important and abundant protein in eukaryotic cells, essential for the activation of a large set of signal transduction and regulatory proteins. During the functional cycle, the Hsp90 dimer performs large conformational rearrangements. The transient N-terminal dimerization of Hsp90 has been extensively investigated, under the assumption that the C-terminal interface is stably dimerized. Using a fluorescence-based single molecule assay and Hsp90 dimers caged in lipid vesicles, we were able to separately observe and kinetically analyze N- and C-terminal dimerizations. Surprisingly, the C-terminal dimer opens and closes with fast kinetics. The occupancy of the unexpected C-terminal open conformation can be modulated by nucleotides bound to the N-terminal domain and by N-terminal deletion mutations, clearly showing a communication between the two terminal domains. Moreover our findings suggest that the C- and N-terminal dimerizations are anticorrelated. This changes our view on the conformational cycle of Hsp90 and shows the interaction of two dimerization domains.

  • FRET
  • cooperativity
  • vesicles
  • intramelocular communication

Footnotes

  • 1To whom correspondence should be addressed. E-mail: thorsten.hugel{at}ph.tum.de.
  • Author contributions: J.B. and T.H. designed research; C.R., M.M., and B.H. performed research; C.R., M.M., B.H., and T.H. analyzed data; and C.R., M.M., J.B., and T.H. wrote the paper.

  • The authors declare no conflict of interest.

  • This article is a PNAS Direct Submission.

  • This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1000916107/-/DCSupplemental.

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    Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
    C. Ratzke, M. Mickler, B. Hellenkamp, J. Buchner, T. Hugel
    Proceedings of the National Academy of Sciences Aug 2010, DOI: 10.1073/pnas.1000916107

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    Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
    C. Ratzke, M. Mickler, B. Hellenkamp, J. Buchner, T. Hugel
    Proceedings of the National Academy of Sciences Aug 2010, DOI: 10.1073/pnas.1000916107
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    Proceedings of the National Academy of Sciences: 118 (3)
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