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TitlePih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p.
Journal, issue, pagesStructure, Vol. 25, Issue 10, Page 1519-11529.e4, Year 2017
Publish dateOct 3, 2017
AuthorsShaoxiong Tian / Ge Yu / Huan He / Yu Zhao / Peilu Liu / Alan G Marshall / Borries Demeler / Scott M Stagg / Hong Li /
PubMed AbstractThe Saccharomyces cerevisiae (Sc) R2TP complex affords an Hsp90-mediated and nucleotide-driven chaperone activity to proteins of small ribonucleoprotein particles (snoRNPs). The current lack of ...The Saccharomyces cerevisiae (Sc) R2TP complex affords an Hsp90-mediated and nucleotide-driven chaperone activity to proteins of small ribonucleoprotein particles (snoRNPs). The current lack of structural information on the ScR2TP complex, however, prevents a mechanistic understanding of this biological process. We characterized the structure of the ScR2TP complex made up of two AAA+ ATPases, Rvb1/2p, and two Hsp90 binding proteins, Tah1p and Pih1p, and its interaction with the snoRNP protein Nop58p by a combination of analytical ultracentrifugation, isothermal titration calorimetry, chemical crosslinking, hydrogen-deuterium exchange, and cryoelectron microscopy methods. We find that Pih1p-Tah1p interacts with Rvb1/2p cooperatively through the nucleotide-sensitive domain of Rvb1/2p. Nop58p further binds Pih1p-Tahp1 on top of the dome-shaped R2TP. Consequently, nucleotide binding releases Pih1p-Tah1p from Rvb1/2p, which offers a mechanism for nucleotide-driven binding and release of snoRNP intermediates.
External linksStructure / PubMed:28919439 / PubMed Central
MethodsEM (single particle)
Resolution14.0 Å
Structure data

EMDB-8839:
The Hsp90 Co-chaperon R2TP Forms a Hexameric Platform
Method: EM (single particle) / Resolution: 14.0 Å

Source
  • Saccharomyces cerevisiae S288c (yeast)

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