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HOP is a monomer: Investigation of the oligomeric state of the co-chaperone HOP by Fang Yi; Ivo Doudevski; Lynne Regan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The co‐chaperone Hsp70‐Hsp90 organizing protein (HOP) plays a central role in protein folding __in vivo,__ binding to both Hsp70 and Hsp90 and bringing them together in a functional complex. Reports in the literature concerning the oligomeric state of HOP have been inconsistent—is it a monomer, dimer, or higher order oligomer? Knowing the oligomeric state of HOP is important, because it places limits on the number and types of multiprotein complexes that can form during the folding cycle. Thus, the number of feasible models is simplified. Here, we explicitly investigate the oligomeric state of HOP using three complementary methods: gel filtration chromatography, sedimentation equilibrium analytical ultracentrifugation (AUC), and an __in vivo__ coexpression assay. We find that HOP does not behave like a monomeric globular protein on gel filtration. Rather its behavior is consistent with it being either an elongated monomer or a dimer. We follow‐up on these studies using sedimentation equilibrium AUC, which separates on the basis of molecular weight (MW), independent of shape. Sedimentation equilibrium AUC clearly shows that HOP is a monomer, with no indication of higher

Who reads HOP is a monomer: Investigation of the oligomeric state of the co-chaperone HOP?

Author

Fang Yi; Ivo Doudevski; Lynne Regan

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)