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- W2057407790 abstract "The twin arginine translocation (Tat) system is a machinery which can translocate folded proteins across energy transducing membranes. Currently it is supposed that Tat substrates bind directly to Tat translocon components before a ApH-driven translocation occurs. In this review, an alternative model is presented which proposes that membrane integration could precede Tat-dependent translocation. This idea is mainly supported by the recent observations of Tat-independent membrane insertion of Tat substrates in vivo and in vitro. Membrane insertion may allow i) a quality control of the folded state by membrane bound proteases like FtsH, ii) the recognition of the membrane spanning signal peptide by Tat system components, and iii) a pulling mechanism of translocation. In some cases of folded Tat substrates, the membrane targeting process may require ATP-dependent N-terminal unfolding-steps." @default.
- W2057407790 created "2016-06-24" @default.
- W2057407790 creator A5054507913 @default.
- W2057407790 creator A5060985280 @default.
- W2057407790 date "2003-01-01" @default.
- W2057407790 modified "2023-09-25" @default.
- W2057407790 title "An alternative model of the twin arginine translocation system" @default.
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- W2057407790 doi "https://doi.org/10.1078/0944-5013-00176" @default.
- W2057407790 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12608575" @default.
- W2057407790 hasPublicationYear "2003" @default.
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