The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1.
Elife
; 72018 11 26.
Article
em En
| MEDLINE
| ID: mdl-30460895
ABSTRACT
The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors. The ~5000 amino-acid AAA+ ATPase Rea1 (or Midasin) generates force to mechanically remove assembly factors from pre-60S particles, which promotes their export to the cytosol. Here we present three Rea1 cryoEM structures. We visualise the Rea1 engine, a hexameric ring of AAA+ domains, and identify an α-helical bundle of AAA2 as a major ATPase activity regulator. The α-helical bundle interferes with nucleotide-induced conformational changes that create a docking site for the substrate binding MIDAS domain on the AAA +ring. Furthermore, we reveal the architecture of the Rea1 linker, which is involved in force generation and extends from the AAA+ ring. The data presented here provide insights into the mechanism of one of the most complex ribosome maturation factors.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Ribossômicas
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Saccharomyces cerevisiae
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RNA Ribossômico
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Trifosfato de Adenosina
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Proteínas de Saccharomyces cerevisiae
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Subunidades Ribossômicas Maiores de Eucariotos
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ATPases Associadas a Diversas Atividades Celulares
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Elife
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
França