Pih1p-Tah1p puts a lid on hexameric AAA+ ATPases Rvb1/2p
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Date
2017
Authors
Tian, Shaoxiong
Yu, Ge
He, Huan
Zhao, Yu
Liu, Peilu
Marshall, Alan G.
Demeler, Borries
Stagg, Scott M.
Li, Hong
Journal Title
Journal ISSN
Volume Title
Publisher
Cell Press
Abstract
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.
Description
Accepted author manuscript
Keywords
Rvb1 , Rvb2 , AAA+ proteins , Cryoelectron microscopy , Fourier transform mass spectrometry , Ion cyclotron resonance , FT-ICR , FTMS , Hydrogen/deuterium exchange , Analytical ultracentrifugation
Citation
Tian, S., Yu, G., He, H., Zhao, Y., Liu, P., Marshall, A. G., Demeler, B., Stagg, S. M., & Li, H. (2017). Pih1p-Tah1p puts a lid on hexameric AAA+ ATPases Rvb1/2p. Structure, 25(10), 1519-1529. http://dx.doi.org/10.1016/j.str.2017.08.002