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Article

A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans-translation.

Proceedings of the National Academy of Sciences of the United States of America - 15 Feb 2005

Sundermeier Thomas R, Dulebohn Daniel P, Cho Hye Jin, Karzai A Wali

Abstract excerpt

SsrA is a versatile RNA molecule found in all bacteria that functions as both a tRNA and an mRNA. SsrA rescues ribosomes stalled on damaged mRNAs and directs the tagging and degradation of their aberrant protein products. Small protein B (SmpB) is required for all known activities of SsrA. The tw...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15699355
DOI: 10.1073/pnas.0409694102
PMCID: PMC549014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15699355-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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A previously uncharacterized role for small protein B (SmpB) in transfer messenger RNA-mediated trans-translation.PMID 15699355Read ↗

Pre-binding of small protein B to a stalled ribosome triggers trans-translation.Semantic proximity Read ↗

SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA).Semantic proximity Read ↗

Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation.Semantic proximity Read ↗

SmpB contributes to reading frame selection in the translation of transfer-messenger RNA.Semantic proximity Read ↗

Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form.Semantic proximity Read ↗

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Ribosomal protein S1 influences trans-translation in vitro and in vivo.Semantic proximity Read ↗

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Importance of the conserved nucleotides around the tRNA-like structure of Escherichia coli transfer-messenger RNA for protein tagging.Semantic proximity Read ↗

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