ArticleMolecular microbiology2011
The translational regulatory function of SecM requires the precise timing of membrane targeting.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery.Nature communications · 2024Article
- Force transduction creates long-ranged coupling in ribosomes stalled by arrest peptides.Biophysical journal · 2021Article
- Article
- Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.The Biochemical journal · 2020Article
- Increased freedom of movement in the nascent chain results in dynamic changes in the structure of the SecM arrest motif.Bioscience reports · 2019Article
- Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.The Journal of biological chemistry · 2018Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo.Science (New York, N.Y.) · 2015Article
- Charge-driven dynamics of nascent-chain movement through the SecYEG translocon.Nature structural & molecular biology · 2015Article
- A simple real-time assay for in vitro translation.RNA (New York, N.Y.) · 2015Article
- Translation initiation rate determines the impact of ribosome stalling on bacterial protein synthesis.The Journal of biological chemistry · 2014Article
- The dynamics of SecM-induced translational stalling.Cell reports · 2014Article
- Mutations in the Escherichia coli ribosomal protein L22 selectively suppress the expression of a secreted bacterial virulence factor.Journal of bacteriology · 2013Article
- A biphasic pulling force acts on transmembrane helices during translocon-mediated membrane integration.Nature structural & molecular biology · 2012Article
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2 authors.
Funding
Abstract
In Escherichia coli, secA expression is regulated at the translational level by an upstream gene (secM) that encodes a presecretory protein. SecM contains a C-terminal sequence motif that induces a transient translation arrest. Inhibition of SecM membrane targeting prolongs the translation arrest and increases SecA synthesis by concomitantly altering the structure of the secM-secA mRNA. Here we show that the SecM signal peptide plays an essential role in this regulatory process by acting as a molecular timer that co-ordinates membrane targeting with the synthesis of the arrest motif. We found that signal peptide mutations that alter targeting kinetics and insertions or deletions that change the distance between the SecM signal peptide and the arrest motif perturb the balance between the onset and release of arrest that is required to regulate SecA synthesis. Furthermore, we found that the strength of the interaction between the ribosome and the SecM arrest motif is calibrated to ensure the release of arrest upon membrane targeting. Our results strongly suggest that several distinctive features of the SecM protein evolved as a consequence of constraints imposed by the ribosome and the Sec machinery.
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