期刊
STRUCTURE
卷 21, 期 10, 页码 1834-1847出版社
CELL PRESS
DOI: 10.1016/j.str.2013.07.024
关键词
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资金
- French Agence Nationale pour la Recherche [ANR 06-BLAN-0208-02, ANR 11 BSV8 015 03, ANR-05-JCJC, 015101]
- French Centre National de la Recherche Scientifique
- Lorraine University
- Plan Etat Region Lorraine (Bioengineering program)
- European EURASNET network [LSHG-CT-2005-518238]
- French Ligue Nationale contre le cancer Grand-Est [30025555]
- French Association pour la Recherche contra le Cancer [SFI20101201793]
- French Ministere de l'Enseignement Superieur et de la Recherche
- EURASNET network
- NCCR-SNF structural biology
- ETH Zurich
- Agence Nationale de la Recherche (ANR) [ANR-06-BLAN-0208] Funding Source: Agence Nationale de la Recherche (ANR)
The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase assembly through interaction with the R2TP complex. This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP. Its minimal TPR domain includes two TPR motifs and a capping helix. We established the high-resolution solution structures of Tah1 free and in complex with the Hsp90 C-terminal peptide. The TPR fold is similar in the free and bound forms and we show experimentally that in addition to its solvating/stabilizing role, the capping helix is essential for the recognition of the Hsp90 (EMEEVD709)-E-704 motif. In addition to Lys79 and Arg83 from the carboxylate clamp, this helix bears Tyr82 forming a pi/S-CH3 interaction with Hsp90 M-705 from the peptide 310 helix. The Tah1 C-terminal region is unfolded, and we demonstrate that it is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding.
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