ArticleJournal of bacteriology2003
Translocon "pulling" of nascent SecM controls the duration of its translational pause and secretion-responsive secA regulation.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 104 citations in OpenAlex.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Structural insights into YheS-mediated release of SecM-arrested ribosome.Nature communications · 2026Article
- Hydrogen/deuterium exchange mass spectrometry analysis of ribosome-nascent chain complexes to study protein biogenesis at the peptide level.Nature protocols · 2026Article
- Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome.Nature communications · 2024Article
- Control of mRNA fate by its encoded nascent polypeptide.Molecular cell · 2023Review
- Cotranslational folding and assembly of the dimericProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Nucleic acids research · 2021Article
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Translational regulation of environmental adaptation in bacteria.The Journal of biological chemistry · 2020Review
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.The Biochemical journal · 2020Article
- Mechanism of ribosome stalling during translation of a poly(A) tail.Nature structural & molecular biology · 2019Article
- Mechanochemistry in Translation.Biochemistry · 2019Review
- Article
- Differences in the path to exit the ribosome across the three domains of life.Nucleic acids research · 2019Article
- Domain topology, stability, and translation speed determine mechanical force generation on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Increased freedom of movement in the nascent chain results in dynamic changes in the structure of the SecM arrest motif.Bioscience reports · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SecA is an ATPase and motor protein that drives protein translocation across the bacterial plasma membrane. In Escherichia coli SecA levels are regulated by the secretion needs of the cell utilizing secM, which encodes a secreted protein. Previous studies demonstrated that this regulation requires a translational pause within secM, whose duration regulates the accessibility of the secA Shine-Dalgarno sequence on secM secA mRNA. Here we provide evidence that translocon "pulling" of nascent SecM is what regulates the duration of the secM translational pause, and thus secA expression levels, thereby providing direct support for this model.
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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.