Centre National de la Recherche Scientifique (CNRS)
ANR-16-CE11-0032-04
フランス
Centre National de la Recherche Scientifique (CNRS)
ANR-23-CE12-0022 YMCR
フランス
Centre National de la Recherche Scientifique (CNRS)
ANR-23-CE44-0035 NAProt-XLMS
フランス
Fundacao para a Ciencia e a Tecnologia
UIDB/04462/2020
ポルトガル
Fundacao para a Ciencia e a Tecnologia
UIDP/04462/2020
ポルトガル
Other government
ProFI - ANR-10-INBS-08-03
Other government
LS4FUTURE - LA/P/0087/2020
引用
ジャーナル: Nat Commun / 年: 2026 タイトル: An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex. 著者: Paulo E Santo / Marie-Eve Chagot / Hugo Gizardin-Fredon / Marie Ley / Thomas Chenuel / Evolène Deslignière / Laura Plassart / Ana C F Paiva / Pedro M F Sousa / Edouard Bertrand / Bruno ...著者: Paulo E Santo / Marie-Eve Chagot / Hugo Gizardin-Fredon / Marie Ley / Thomas Chenuel / Evolène Deslignière / Laura Plassart / Ana C F Paiva / Pedro M F Sousa / Edouard Bertrand / Bruno Charpentier / Céline Verheggen / Marc Quinternet / Philippe Meyer / Tiago M Bandeiras / Sarah Cianférani / Célia Plisson-Chastang / Xavier Manival / 要旨: R2SP belongs to the R2TP-like quaternary chaperone family and consists of RUVBL1/RUVBL2 AAA+ ATPases, which powers the machinery, and SPAG1 and PIH1D2 adapter proteins that engage specific clients to ...R2SP belongs to the R2TP-like quaternary chaperone family and consists of RUVBL1/RUVBL2 AAA+ ATPases, which powers the machinery, and SPAG1 and PIH1D2 adapter proteins that engage specific clients to promote their quaternary assembly. However, little is known about the structure of R2SP and the precise mode of action of these R2TP-like complexes. Here, we combined biochemical (ATPase and fluorescence polarization assays) and structural approaches (NMR, structural mass spectrometry, cryo-EM) to investigate the 3D organization of the R2SP complex, its mode of assembly and ATPase activity. Together with our binding, mutational and kinetic studies, these results led us to propose a model in which SPAG1 and PIH1D2 bind and cooperatively engage RUVBL1/RUVBL2 to produce R2SP. This reveals a 3D structure close to the canonical R2TP complex but also highlights differences in RUVBL1/RUVBL2 ATPase activity, as well as the cooperative binding of SPAG1 and PIH1D2 to this catalytic core that may explain functional difference between the two systems.
全体 : Hexameric RuvBL1/RuvBL2 complex bound to C-terminal Reagion of SPAG1
全体
名称: Hexameric RuvBL1/RuvBL2 complex bound to C-terminal Reagion of SPAG1
要素
複合体: Hexameric RuvBL1/RuvBL2 complex bound to C-terminal Reagion of SPAG1
複合体: Components that form the hexameric Ring
タンパク質・ペプチド: RuvB-like 1
タンパク質・ペプチド: RuvB-like 2
タンパク質・ペプチド: Sperm-associated antigen 1
リガンド: ADENOSINE-5'-DIPHOSPHATE
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超分子 #1: Hexameric RuvBL1/RuvBL2 complex bound to C-terminal Reagion of SPAG1
超分子
名称: Hexameric RuvBL1/RuvBL2 complex bound to C-terminal Reagion of SPAG1 タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#3 詳細: Co-expressed RuvBL1/2 complex incubated with co-expressed SPAG1/PIH1D2 complex
由来(天然)
生物種: Homo sapiens (ヒト)
分子量
理論値: 338 KDa
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超分子 #2: Components that form the hexameric Ring
超分子
名称: Components that form the hexameric Ring / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #1-#2 詳細: RuvBL1 (Chains A-C), amino acids 125-235, and RuvBL2 (Chain E), amino acids 133-238, are present in this model, although the final PostProcess map lacks sufficient density. These reagions ...詳細: RuvBL1 (Chains A-C), amino acids 125-235, and RuvBL2 (Chain E), amino acids 133-238, are present in this model, although the final PostProcess map lacks sufficient density. These reagions were rigid fitted in the Refine Map (Reference models 2C9O for RuvBL1 and 6H7X for RuvBL2).