Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.
Mol Cell
; 81(1): 115-126.e7, 2021 01 07.
Article
em En
| MEDLINE
| ID: mdl-33259810
ABSTRACT
In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Bacillus subtilis
/
Proteínas de Bactérias
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Subunidades Ribossômicas Maiores de Bactérias
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Alemanha