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Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM.

Sci Adv. 2019-05; 
Mu?oz-HernándezHugo,PalMohinder,RodríguezCarlos F,Fernandez-LeiroRafael,ProdromouChrisostomos,PearlLaurence H,LlorcaO
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Recombinant Proteins RPAP3 and PIH1D1 were cloned containing an N-terminal GST and 6×His-tag, respectively. We purchased RPAP3 from GenScript Get A Quote

摘要

The human R2TP complex (RUVBL1-RUVBL2-RPAP3-PIH1D1) is an HSP90 co-chaperone required for the maturation of several essential multiprotein complexes, including RNA polymerase II, small nucleolar ribonucleoproteins, and PIKK complexes such as mTORC1 and ATR-ATRIP. RUVBL1-RUVBL2 AAA-ATPases are also primary components of other essential complexes such as INO80 and Tip60 remodelers. Despite recent efforts, the molecular mechanisms regulating RUVBL1-RUVBL2 in these complexes remain elusive. Here, we report cryo-EM structures of R2TP and show how access to the nucleotide-binding site of RUVBL2 is coupled to binding of the client recruitment component of R2TP (PIH1D1) to its DII domain. This interaction ind... More

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