The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones

The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones

R2TP is an HSP90 co-chaperone composed of an RPAP3-PIH1D1 heterodimer, which binds two essential AAA+ ATPases RUVBL1/RUVBL2. Here authors use a structural approach to study RPAP3 and find an RPAP3-like protein (SPAG1) which also forms a co-chaperone complex with PIH1D2 and RUVBL1/2 enriched in testi...

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Auteurs principaux: Chloé Maurizy, Marc Quinternet, Yoann Abel, Céline Verheggen, Paulo E. Santo, Maxime Bourguet, Ana C.F. Paiva, Benoît Bragantini, Marie-Eve Chagot, Marie-Cécile Robert, Claire Abeza, Philippe Fabre, Philippe Fort, Franck Vandermoere, Pedro M.F. Sousa, Jean-Christophe Rain, Bruno Charpentier, Sarah Cianférani, Tiago M. Bandeiras, Bérengère Pradet-Balade, Xavier Manival, Edouard Bertrand
Format: article
Langue:EN
Publié: Nature Portfolio 2018
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Science
Q
Accès en ligne:https://doaj.org/article/f9bce095aa2a4c49a49a7a66e4c6ecf6
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Résumé:R2TP is an HSP90 co-chaperone composed of an RPAP3-PIH1D1 heterodimer, which binds two essential AAA+ ATPases RUVBL1/RUVBL2. Here authors use a structural approach to study RPAP3 and find an RPAP3-like protein (SPAG1) which also forms a co-chaperone complex with PIH1D2 and RUVBL1/2 enriched in testis.

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