ArticleJournal of molecular biology2009
SmpB contributes to reading frame selection in the translation of transfer-messenger RNA.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Structures of tmRNA and SmpB as they transit through the ribosome.Nature communications · 2021Article
- Small protein B upregulates sensor kinase bvgS expression in Aeromonas veronii.Frontiers in microbiology · 2015Article
- Mechanism of trans-translation revealed by in vitro studies.Frontiers in microbiology · 2014Review
- The SmpB C-terminal tail helps tmRNA to recognize and enter stalled ribosomes.Frontiers in microbiology · 2014Review
- Biochemical aspects of bacterial strategies for handling the incomplete translation processes.Frontiers in microbiology · 2014Review
- Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB.Frontiers in microbiology · 2014Review
- Active and accurate trans-translation requires distinct determinants in the C-terminal tail of SmpB protein and the mRNA-like domain of transfer messenger RNA (tmRNA).The Journal of biological chemistry · 2013Article
- Article
- The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012Review
- The role of SmpB and the ribosomal decoding center in licensing tmRNA entry into stalled ribosomes.RNA (New York, N.Y.) · 2011Article
- tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation.Journal of nucleic acids · 2011Article
- Article
- tmRNA-SmpB: a journey to the centre of the bacterial ribosome.The EMBO journal · 2010Article
- Visualizing the transfer-messenger RNA as the ribosome resumes translation.The EMBO journal · 2010Article
- rRNA mutations that inhibit transfer-messenger RNA activity on stalled ribosomes.Journal of bacteriology · 2010Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transfer-messenger RNA (tmRNA) acts first as a tRNA and then as an mRNA template to rescue stalled ribosomes in eubacteria. Together with its protein partner, SmpB (small protein B), tmRNA enters stalled ribosomes and transfers an Ala residue to the growing polypeptide chain. A remarkable step then occurs: the ribosome leaves the stalled mRNA and resumes translation using tmRNA as a template, adding a short peptide tag that destines the aborted protein for destruction. Exactly how the ribosome switches templates, resuming translation on tmRNA in the proper reading frame, remains unknown. Within the tmRNA sequence itself, five nucleotides (U85AGUC) immediately upstream of the first codon appear to direct frame selection. In particular, mutation of the conserved A86 results in severe loss of function both in vitro and in vivo. The A86C mutation causes translation to resume exclusively in the +1 frame. Several candidate binding partners for this upstream sequence have been identified in vitro. Using a genetic selection for tmRNA activity in Escherichia coli, we identified mutations in the SmpB protein that restore the function of A86C tmRNA in vivo. The SmpB mutants increase tagging in the normal reading frame and reduce tagging in the +1 frame. These results demonstrate that SmpB is functionally linked with the sequence upstream of the tmRNA template; both contribute to reading frame selection on tmRNA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.