A filamentous molecular chaperone of the prefoldin family from the deep‐sea hyperthermophile Methanocaldococcus jannaschii Journal Article uri icon



  • AbstractPrefoldin 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, γ 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, α and β PFD, into Eschericia coli and characterized the proteins. Whereas α and β PFD readily assembled into the expected hexamer, γ PFD would not assemble with either protein. Instead, γ PFD forms long filaments of defined dimensions measuring 8.5 nm × 1.7–3.5 nm and lengths exceeding 1 μm. Filamentous γ 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.

publication date

  • April 1, 2007

has restriction

  • bronze

Date in CU Experts

  • September 24, 2019 5:15 AM

Full Author List

  • Whitehead TA; Boonyaratanakornkit BB; Höllrigl V; Clark DS

author count

  • 4

Other Profiles

International Standard Serial Number (ISSN)

  • 0961-8368

Electronic International Standard Serial Number (EISSN)

  • 1469-896X

Additional Document Info

start page

  • 626

end page

  • 634


  • 16


  • 4