Cell Stress and Chaperones

, 14:629

Novel Hsp90 partners discovered using complementary proteomic approaches

  • Pavel A. Tsaytler
  • Jeroen Krijgsveld
  • Soenita S. Goerdayal
  • Stefan Rüdiger
  • Maarten R. Egmond
Original Paper

DOI: 10.1007/s12192-009-0115-z

Cite this article as:
Tsaytler, P.A., Krijgsveld, J., Goerdayal, S.S. et al. Cell Stress and Chaperones (2009) 14: 629. doi:10.1007/s12192-009-0115-z

Abstract

Hsp90 is an essential eukaryotic molecular chaperone that stabilizes a large set of client proteins, many of which are involved in various cellular signaling pathways. The current list of Hsp90 interactors comprises about 200 proteins and this number is growing steadily. In this paper, we report on the application of three complementary proteomic approaches directed towards identification of novel proteins that interact with Hsp90. These methods are coimmunoprecipitation, pull down with biotinylated geldanamycin, and immobilization of Hsp90β on sepharose. In all, this study led to the identification of 42 proteins, including 18 proteins that had not been previously characterized as Hsp90 interactors. These novel Hsp90 partners not only represent abundant protein species, but several proteins were identified at low levels, among which signaling kinase Cdk3 and putative transcription factor tripartite motif-containing protein 29. Identification of tetratricopeptide-repeat-containing mitochondrial import receptor protein Tom34 suggests the involvement of Hsp90 in the early steps of translocation of mitochondrial preproteins. Taken together, our data expand the knowledge of the Hsp90 interactome and provide a further step in our understanding of the Hsp90 chaperone system.

Keywords

Heat shock protein 90 Identification Immobilization Interactome Kinase Partners 

Abbreviations

ACN

acetonitrile

Cdk3

cyclin-dependent kinase 3

CNBr

cyanogen bromide

DSP

Dithiobis[succinimidyl propionate]

GA

geldanamycin

Copyright information

© Cell Stress Society International 2009

Authors and Affiliations

  • Pavel A. Tsaytler
    • 1
  • Jeroen Krijgsveld
    • 2
  • Soenita S. Goerdayal
    • 2
  • Stefan Rüdiger
    • 3
  • Maarten R. Egmond
    • 1
  1. 1.Department of Membrane Enzymology, Bijvoet Center for Biomolecular ResearchUtrecht UniversityUtrechtthe Netherlands
  2. 2.Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical SciencesUtrecht UniversityUtrechtthe Netherlands
  3. 3.Department Cellular Protein Chemistry, Bijvoet Center for Biomolecular ResearchUtrecht UniversityUtrechtthe Netherlands

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