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Protein Science (2007), 16:626-634. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii

Timothy A. Whitehead, Boonchai B. Boonyaratanakornkit, Volker Höllrigl1, and Douglas S. Clark1

Department of Chemical Engineering, University of California, Berkeley, Berkeley, California 94720, USA

(RECEIVED October 3, 2006; FINAL REVISION December 16, 2006; ACCEPTED December 22, 2006)

Prefoldin is a molecular chaperone found in the domains eukarya and archaea that acts in conjunction with Group II chaperonin to correctly fold other nascent proteins. Previously, our group identified a putative single subunit of prefoldin, {gamma} PFD, that was up-regulated in response to heat stress in the hyperthermophilic archaeon Methanocaldococcus jannaschii. In order to characterize this protein, we subcloned and expressed it and the other two prefoldin subunits from M. jannaschii, {alpha} and beta PFD, into Eschericia coli and characterized the proteins. Whereas {alpha} and beta PFD readily assembled into the expected hexamer, {gamma} PFD would not assemble with either protein. Instead, {gamma} PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7–3.5 nm and lengths exceeding 1 µm. Filamentous {gamma} PFD acts as a molecular chaperone through in vitro assays, in a manner comparable to PFD. A possible molecular model for filament assembly is discussed.

Keywords: prefoldin; molecular chaperones; protein filaments; heat-shock response


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