Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Elite
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Hela Cell
SUBMITTER: Franck Vandermoere
LAB HEAD: Edouard Bertrand
PROVIDER: PXD009499 | Pride | 2018-06-10
REPOSITORIES: pride
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Maurizy Chloé C Quinternet Marc M Abel Yoann Y Verheggen Céline C Santo Paulo E PE Bourguet Maxime M C F Paiva Ana A Bragantini Benoît B Chagot Marie-Eve ME Robert Marie-Cécile MC Abeza Claire C Fabre Philippe P Fort Philippe P Vandermoere Franck F M F Sousa Pedro P Rain Jean-Christophe JC Charpentier Bruno B Cianférani Sarah S Bandeiras Tiago M TM Pradet-Balade Bérengère B Manival Xavier X Bertrand Edouard E
Nature communications 20180529 1
R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like ...[more]