ArticleJournal of molecular biology2015
SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Features of membrane protein sequence direct post-translational insertion.Nature communications · 2024Article
- Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking and LTA synthesis.bioRxiv : the preprint server for biology · 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
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- The BB0345 Hypothetical Protein of Borrelia burgdorferi Is Essential for Mammalian Infection.Infection and immunity · 2020Article
- Interactions Screenings Unearth Potential New Divisome Components in theMicroorganisms · 2019Article
- Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Dropping Out and Other Fates of Transmembrane Segments Inserted by the SecA ATPase.Journal of molecular biology · 2019Article
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- SecA mediates cotranslational targeting and translocation of an inner membrane protein.The Journal of cell biology · 2017Article
- The bacterial Sec system is required for the organization and function of the MreB cytoskeleton.PLoS genetics · 2017Article
- SecA-a New Twist in the Tale.Journal of bacteriology · 2017Article
- Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS.Journal of molecular microbiology and biotechnology · 2017Article
- Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Molecular oral microbiology · 2015Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The transmembrane (TM) helices of most type II single-span membrane proteins (S-SMPs) of Escherichia coli occur near the N-terminus, where the cell's targeting mechanisms can readily identify it as it emerges from the ribosome. However, the TM helices of a few S-SMPs, such as RodZ, occur a hundred or more residues downstream from the N-terminus, which raises fundamental questions about targeting and assembly. Because of RodZ's novelty and potential usefulness for understanding TM helix insertion in vivo, we examined its membrane targeting and assembly. We used RodZ constructs containing immunotags before the TM domain to assess membrane insertion using proteinase K digestion. We confirmed the N(in)-C(out) (type II) topology of RodZ and established the absence of a targeting signal other than the TM domain. RodZ was not inserted into the membrane under SecA depletion conditions or in the presence of sodium azide, which is known to inhibit SecA. Insertion failed when the TM proton gradient was abolished with Carbonyl cyanide m-chlorophenyl hydrazone. Insertion also failed when RodZ was expressed in SecE-depleted E. coli, indicating that the SecYEG translocon is required for RodZ assembly. Protease accessibility assays of RodZ in other E. coli depletion strains revealed that insertion is independent of SecB, YidC, and SecD/F. Insertion was found to be only weakly dependent on the signal recognition particle pathway: insertion was weakly dependent on the Ffh but independent of FtsY. We conclude that membrane insertion of RodZ requires only the SecYEG translocon, the SecA ATPase motor, and the TM proton motive force.
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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.