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- W3112907801 abstract "Bacterial cells utilize monitoring substrates, which undergo force-sensitive translation elongation arrest, to feedback-regulate a Sec-related gene. Vibrio alginolyticus VemP controls the expression of SecD/F that stimulates a late step of translocation by undergoing export-regulated elongation arrest. Here, we attempted at delineating the pathway of the VemP nascent-chain interaction with Sec-related factors, and identified the signal recognition particle (SRP) and PpiD (a membrane-anchored periplasmic chaperone) in addition to other translocon components and a ribosomal protein as interacting partners. Our results showed that SRP is required for the membrane-targeting of VemP, whereas PpiD acts cooperatively with SecD/F in the translocation and arrest-cancelation of VemP. We also identified the conserved Arg-85 residue of VemP as a crucial element that confers PpiD-dependence to VemP and plays an essential role in the regulated arrest-cancelation. We propose a scheme of the arrest-cancelation processes of VemP, which likely monitors late steps in the protein translocation pathway." @default.
- W3112907801 created "2020-12-21" @default.
- W3112907801 creator A5055113366 @default.
- W3112907801 creator A5063763043 @default.
- W3112907801 creator A5083290807 @default.
- W3112907801 date "2020-12-15" @default.
- W3112907801 modified "2023-09-30" @default.
- W3112907801 title "Fine interaction profiling of VemP and mechanisms responsible for its translocation-coupled arrest-cancelation" @default.
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- W3112907801 doi "https://doi.org/10.7554/elife.62623" @default.
- W3112907801 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7793623" @default.
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- W3112907801 hasPublicationYear "2020" @default.
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