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Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP.

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Crowe-McAuliffe C,Takada H,Murina V,Polte C,Kasvandik S,Tenson T,Ignatova Z,Atkinson GC,Wilson DN,Hauryliuk V

doi

10.1016/j.molcel.2020.11.002

subject

Has Abstract

pub_date

2021-01-07 00:00:00

pages

115-126.e7

issue

1

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(20)30780-2

journal_volume

81

pub_type

杂志文章

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