6ez4
NMR structure of the C-terminal domain of the human RPAP3 proteinNMR structure of the C-terminal domain of the human RPAP3 protein
Structural highlights
Function[RPAP3_HUMAN] Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.[1] Publication Abstract from PubMedR2TP 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 protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-alpha2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha2 expression and for the assembly of liprin-alpha2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis. The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.,Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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