ArticleProceedings of the National Academy of Sciences of the United States of America2015
Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.
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36 citing papers in PubMed, 71 citations in OpenAlex.
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM.Nature communications · 2026Article
- Evolutionary adaptation of bacterial proteomes to translation-impeding sequences.The EMBO journal · 2026Article
- A mini-hairpin shaped nascent peptide blocks translation termination by a distinct mechanism.Nature communications · 2025Article
- Effect of Translation-Enhancing Nascent SKIK Peptide on the Arrest Peptides Containing Consecutive Proline.ACS synthetic biology · 2024Article
- Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding.Journal of chemical information and modeling · 2024Article
- The ABCF proteins in Escherichia coli individually cope with 'hard-to-translate' nascent peptide sequences.Nucleic acids research · 2024Article
- Patchy and widespread distribution of bacterial translation arrest peptides associated with the protein localization machinery.Nature communications · 2024Article
- RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity.Nature communications · 2024Article
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- Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel.Nucleic acids research · 2022Article
- Peptidyl transferase center decompaction and structural constraints during early protein elongation on the ribosome.Scientific reports · 2021Article
- Nascent polypeptide within the exit tunnel stabilizes the ribosome to counteract risky translation.The EMBO journal · 2021Article
- Dispatched uses NaNature · 2021Article
- Force transduction creates long-ranged coupling in ribosomes stalled by arrest peptides.Biophysical journal · 2021Article
- Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Nucleic acids research · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
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- Ribosome-associated quality control of membrane proteins at the endoplasmic reticulum.Journal of cell science · 2020Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SecDF interacts with the SecYEG translocon in bacteria and enhances protein export in a proton-motive-force-dependent manner. Vibrio alginolyticus, a marine-estuarine bacterium, contains two SecDF paralogs, V.SecDF1 and V.SecDF2. Here, we show that the export-enhancing function of V.SecDF1 requires Na+ instead of H+, whereas V.SecDF2 is Na+-independent, presumably requiring H+. In accord with the cation-preference difference, V.SecDF2 was only expressed under limited Na+ concentrations whereas V.SecDF1 was constitutive. However, it is not the decreased concentration of Na+ per se that the bacterium senses to up-regulate the V.SecDF2 expression, because marked up-regulation of the V.SecDF2 synthesis was observed irrespective of Na+ concentrations under certain genetic/physiological conditions: (i) when the secDF1VA gene was deleted and (ii) whenever the Sec export machinery was inhibited. VemP (Vibrio export monitoring polypeptide), a secretory polypeptide encoded by the upstream ORF of secDF2VA, plays the primary role in this regulation by undergoing regulated translational elongation arrest, which leads to unfolding of the Shine-Dalgarno sequence for translation of secDF2VA. Genetic analysis of V. alginolyticus established that the VemP-mediated regulation of SecDF2 is essential for the survival of this marine bacterium in low-salinity environments. These results reveal that a class of marine bacteria exploits nascent-chain ribosome interactions to optimize their protein export pathways to propagate efficiently under different ionic environments that they face in their life cycles.
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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.