Pih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p.

Shaoxiong Tian, Ge Yu, Huan He, Yu Zhao, Peilu Liu, Alan G Marshall, Borries Demeler, Scott M Stagg, Hong Li

Structure (London, England : 1993) 2017 Oct 03

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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. Copyright © 2017 Elsevier Ltd. All rights reserved.

Citation

Shaoxiong Tian, Ge Yu, Huan He, Yu Zhao, Peilu Liu, Alan G Marshall, Borries Demeler, Scott M Stagg, Hong Li. Pih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p. Structure (London, England : 1993). 2017 Oct 03;25(10):1519-1529.e4