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Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation.
- Source :
-
The EMBO journal [EMBO J] 2021 Dec 01; Vol. 40 (23), pp. e108299. Date of Electronic Publication: 2021 Oct 20. - Publication Year :
- 2021
-
Abstract
- 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.<br /> (© 2021 The Authors.)
- Subjects :
- Escherichia coli genetics
Escherichia coli Proteins genetics
Peptides genetics
Ribosomal Proteins genetics
Ribosomes genetics
Ribosomes metabolism
Escherichia coli metabolism
Escherichia coli Proteins metabolism
Open Reading Frames
Peptides metabolism
Protein Biosynthesis
Ribosomal Proteins metabolism
Ribosomes chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1460-2075
- Volume :
- 40
- Issue :
- 23
- Database :
- MEDLINE
- Journal :
- The EMBO journal
- Publication Type :
- Academic Journal
- Accession number :
- 34672004
- Full Text :
- https://doi.org/10.15252/embj.2021108299