The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry
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Carla Schmidt1, Victoria Beilsten-Edmands1 and Carol V. Robinson1
1 Department of Chemistry, University of Oxford, Oxford, UK
Carol V. Robinson, email:
Keywords: Hsp70/90 chaperone cycle, co-chaperones, client proteins, mass spectrometry, cross-linking
Received: June 03, 2015 Accepted: June 30, 2015 Published: July 22, 2015
The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52. Because of the many proteins involved in these interactions it is often difficult to delineate all possible combinations of subunits in the complexes formed. We employed mass spectrometry to monitor the assembly and to determine the favoured pathways within these chaperone cycles. Combining the subunit composition with chemical cross-linking and proteomics allowed us to define interaction interfaces, protein dynamics and new intermediates.
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