Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation.
cell-free translation
nascent polypeptide chain
polypeptidyl-tRNA
ribosomal exit tunnel
ribosome
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
01 12 2021
01 12 2021
Historique:
revised:
21
09
2021
received:
18
03
2021
accepted:
29
09
2021
pubmed:
22
10
2021
medline:
22
12
2021
entrez:
21
10
2021
Statut:
ppublish
Résumé
Continuous translation elongation, irrespective of amino acid sequences, is a prerequisite for living organisms to produce their proteomes. However, nascent polypeptide products bear an inherent risk of elongation abortion. For example, negatively charged sequences with occasional intermittent prolines, termed intrinsic ribosome destabilization (IRD) sequences, weaken the translating ribosomal complex, causing certain nascent chain sequences to prematurely terminate translation. Here, we show that most potential IRD sequences in the middle of open reading frames remain cryptic and do not interrupt translation, due to two features of the nascent polypeptide. Firstly, the nascent polypeptide itself spans the exit tunnel, and secondly, its bulky amino acid residues occupy the tunnel entrance region, thereby serving as a bridge and protecting the large and small ribosomal subunits from dissociation. Thus, nascent polypeptide products have an inbuilt ability to ensure elongation continuity.
Identifiants
pubmed: 34672004
doi: 10.15252/embj.2021108299
pmc: PMC8634131
doi:
Substances chimiques
Escherichia coli Proteins
0
Peptides
0
Ribosomal Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e108299Informations de copyright
© 2021 The Authors.
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