TY - JOUR
T1 - NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis
AU - Abel, Yoann
AU - Paiva, Ana C.F.
AU - Bizarro, Jonathan
AU - Chagot, Marie Eve
AU - Santo, Paulo E.
AU - Robert, Marie Cécile
AU - Quinternet, Marc
AU - Vandermoere, Franck
AU - Sousa, Pedro M.F.
AU - Fort, Philippe
AU - Charpentier, Bruno
AU - Manival, Xavier
AU - Bandeiras, Tiago M.
AU - Bertrand, Edouard
AU - Verheggen, Céline
N1 - Publisher Copyright:
© 2021 The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2021/1/25
Y1 - 2021/1/25
N2 - The PAQosome is a large complex composed of the HSP90/R2TP chaperone and a prefoldin-like module. It promotes the biogenesis of cellular machineries but it is unclear how it discriminates closely related client proteins. Among the main PAQosome clients are C/D snoRNPs and in particular their core protein NOP58. Using NOP58 mutants and proteomic experiments, we identify different assembly intermediates and show that C12ORF45, which we rename NOPCHAP1, acts as a bridge between NOP58 and PAQosome. NOPCHAP1 makes direct physical interactions with the CC-NOP domain of NOP58 and domain II of RUVBL1/2 AAA+ ATPases. Interestingly, NOPCHAP1 interaction with RUVBL1/2 is disrupted upon ATP binding. Moreover, while it robustly binds both yeast and human NOP58, it makes little interactions with NOP56 and PRPF31, two other closely related CC-NOP proteins. Expression of NOP58, but not NOP56 or PRPF31, is decreased in NOPCHAP1 KO cells. We propose that NOPCHAP1 is a client-loading PAQosome cofactor that selects NOP58 to promote box C/D snoRNP assembly.
AB - The PAQosome is a large complex composed of the HSP90/R2TP chaperone and a prefoldin-like module. It promotes the biogenesis of cellular machineries but it is unclear how it discriminates closely related client proteins. Among the main PAQosome clients are C/D snoRNPs and in particular their core protein NOP58. Using NOP58 mutants and proteomic experiments, we identify different assembly intermediates and show that C12ORF45, which we rename NOPCHAP1, acts as a bridge between NOP58 and PAQosome. NOPCHAP1 makes direct physical interactions with the CC-NOP domain of NOP58 and domain II of RUVBL1/2 AAA+ ATPases. Interestingly, NOPCHAP1 interaction with RUVBL1/2 is disrupted upon ATP binding. Moreover, while it robustly binds both yeast and human NOP58, it makes little interactions with NOP56 and PRPF31, two other closely related CC-NOP proteins. Expression of NOP58, but not NOP56 or PRPF31, is decreased in NOPCHAP1 KO cells. We propose that NOPCHAP1 is a client-loading PAQosome cofactor that selects NOP58 to promote box C/D snoRNP assembly.
UR - http://www.scopus.com/inward/record.url?scp=85100362108&partnerID=8YFLogxK
U2 - 10.1093/nar/gkaa1226
DO - 10.1093/nar/gkaa1226
M3 - Article
C2 - 33367824
AN - SCOPUS:85100362108
SN - 0305-1048
VL - 49
SP - 1094
EP - 1113
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 2
ER -