ArticleStructure (London, England : 1993)2017
Pih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex.Nature communications · 2026Article
- Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024Article
- The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophysical reviews · 2023Review
- TTT (Tel2-Tti1-Tti2) Complex, the Co-Chaperone of PIKKs and a Potential Target for Cancer Chemotherapy.International journal of molecular sciences · 2023Review
- Article
- The Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization.Biomolecules · 2022Review
- Structure of the TELO2-TTI1-TTI2 complex and its function in TOR recruitment to the R2TP chaperone.Cell reports · 2021Article
- NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.Nucleic acids research · 2021Article
- RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes.Cells · 2020Review
- Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p.Scientific reports · 2019Article
- Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function.Biophysical reviews · 2019Review
- Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM.Science advances · 2019Article
- Revealing the architecture of protein complexes by an orthogonal approach combining HDXMS, CXMS, and disulfide trapping.Nature protocols · 2018Article
- The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.Nature communications · 2018Article
- RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.Nature communications · 2018Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.