ArticleThe Journal of cell biology2017
SecA mediates cotranslational targeting and translocation of an inner membrane protein.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Shaping the composition of the mitochondrial outer membrane.Nature cell biology · 2025Review
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- Features of membrane protein sequence direct post-translational insertion.Nature communications · 2024Article
- The biogenesis and maintenance of PSII: Recent advances and current challenges.The Plant cell · 2024Review
- Thylakoid protein FPB1 synergistically cooperates with PAM68 to promote CP47 biogenesis and Photosystem II assembly.Nature communications · 2024Article
- Ribosome profiling reveals multiple roles of SecA in cotranslational protein export.Nature communications · 2022Article
- Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification.Journal of molecular biology · 2022Article
- The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022Review
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021Review
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- Translational Control of Secretory Proteins in Health and Disease.International journal of molecular sciences · 2020Review
- Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Protein targeting to the bacterial plasma membrane was generally thought to occur via two major pathways: cotranslational targeting by signal recognition particle (SRP) and posttranslational targeting by SecA and SecB. Recently, SecA was found to also bind ribosomes near the nascent polypeptide exit tunnel, but the function of this SecA-ribosome contact remains unclear. In this study, we show that SecA cotranslationally recognizes the nascent chain of an inner membrane protein, RodZ, with high affinity and specificity. In vitro reconstitution and in vivo targeting assays show that SecA is necessary and sufficient to direct the targeting and translocation of RodZ to the bacterial plasma membrane in an obligatorily cotranslational mechanism. Sequence elements upstream and downstream of the RodZ transmembrane domain dictate nascent polypeptide selection by SecA instead of the SRP machinery. These findings identify a new route for the targeting of inner membrane proteins in bacteria and highlight the diversity of targeting pathways that enables an organism to accommodate diverse nascent proteins.
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Registered trials
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