Idioma:

NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis

Abel, Yoann ; Paiva, Ana C F ; Bizarro, Jonathan ; Chagot, Marie-Eve ; Santo, Paulo E ; Robert, Marie-Cécile ; Quinternet, Marc ; Vandermoere, Franck ; Sousa, Pedro M F ; Fort, Philippe ; Charpentier, Bruno ; Manival, Xavier ; Bandeiras, Tiago M ; Bertrand, Edouard ; Verheggen, Céline

Nucleic acids research, 2021-01, Vol.49 (2), p.1094-1113 [Periódico revisado por pares]

England: Oxford University Press

Texto completo disponível

Citações Citado por

Enviar para

Título:
NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis
Autor: Abel, Yoann ; Paiva, Ana C F ; Bizarro, Jonathan ; Chagot, Marie-Eve ; Santo, Paulo E ; Robert, Marie-Cécile ; Quinternet, Marc ; Vandermoere, Franck ; Sousa, Pedro M F ; Fort, Philippe ; Charpentier, Bruno ; Manival, Xavier ; Bandeiras, Tiago M ; Bertrand, Edouard ; Verheggen, Céline
Assuntos: Adenosine Triphosphate - metabolism ; ATPases Associated with Diverse Cellular Activities - metabolism ; Carrier Proteins - metabolism ; DNA Helicases - metabolism ; Eye Proteins - metabolism ; Gene Knockout Techniques ; Genes, Reporter ; HeLa Cells ; HSP90 Heat-Shock Proteins - metabolism ; Humans ; Life Sciences ; Molecular Chaperones - metabolism ; Multiprotein Complexes ; Nuclear Proteins - metabolism ; Protein Domains ; Protein Interaction Mapping ; Proteomics - methods ; Recombinant Fusion Proteins - metabolism ; Ribonucleoproteins, Small Nucleolar - biosynthesis ; Ribonucleoproteins, Small Nucleolar - metabolism ; RNA and RNA-protein complexes ; Saccharomyces cerevisiae Proteins - metabolism
É parte de: Nucleic acids research, 2021-01, Vol.49 (2), p.1094-1113
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMCID: PMC7826282
USDOE Office of Nuclear Energy (NE), Nuclear Fuel Cycle and Supply Chain
PTDC/BBB-BEP/1463/2014
Descrição: Abstract 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.
Editor: England: Oxford University Press
Idioma: Inglês

Links

Voltar para lista de resultados

Anterior Resultado 10 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis

Abel, Yoann ; Paiva, Ana C F ; Bizarro, Jonathan ; Chagot, Marie-Eve ; Santo, Paulo E ; Robert, Marie-Cécile ; Quinternet, Marc ; Vandermoere, Franck ; Sousa, Pedro M F ; Fort, Philippe ; Charpentier, Bruno ; Manival, Xavier ; Bandeiras, Tiago M ; Bertrand, Edouard ; Verheggen, Céline

England: Oxford University Press

Buscando em bases de dados remotas. Favor aguardar.