Pih1p-Tah1p puts a lid on hexameric AAA+ ATPases Rvb1/2p

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dc.contributor.authorTian, Shaoxiong
dc.contributor.authorYu, Ge
dc.contributor.authorHe, Huan
dc.contributor.authorZhao, Yu
dc.contributor.authorLiu, Peilu
dc.contributor.authorMarshall, Alan G.
dc.contributor.authorDemeler, Borries
dc.contributor.authorStagg, Scott M.
dc.contributor.authorLi, Hong
dc.date.accessioned2021-08-13T19:54:18Z
dc.date.available2021-08-13T19:54:18Z
dc.date.issued2017
dc.descriptionAccepted author manuscripten_US
dc.description.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 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.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationTian, 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.2017.08.002en_US
dc.identifier.urihttps://hdl.handle.net/10133/5998
dc.language.isoen_USen_US
dc.publisherCell Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionFlorida State Universityen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttp://dx.doi.org/10.1016/j.str.2017.08.002en_US
dc.subjectRvb1en_US
dc.subjectRvb2en_US
dc.subjectAAA+ proteinsen_US
dc.subjectCryoelectron microscopyen_US
dc.subjectFourier transform mass spectrometryen_US
dc.subjectIon cyclotron resonanceen_US
dc.subjectFT-ICRen_US
dc.subjectFTMSen_US
dc.subjectHydrogen/deuterium exchangeen_US
dc.subjectAnalytical ultracentrifugationen_US
dc.titlePih1p-Tah1p puts a lid on hexameric AAA+ ATPases Rvb1/2pen_US
dc.typeArticleen_US
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