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- W2036762805 abstract "Significance In this paper, we describe the biophysical properties, stoichiometry, and activity of the Escherichia coli SecYEG–SecDF–YajC–YidC holo-translocon. This multiprotein complex consists of seven membrane protein subunits, including those components responsible for both protein secretion (SecYEG) and membrane protein insertion (YidC). We demonstrate the isolation of a stable complex containing YidC together with the core SecY translocon. The availability of this intact assembly allows us to reconstitute posttranslational protein export and cotranslational membrane protein insertion from purified components of known stoichiometry. The experiments demonstrate that protein secretion and insertion occur through a single complex. The reconstitution of membrane protein insertion from defined components is a novel development, breaking ground for the functional analysis of this largely unknown process." @default.
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- W2036762805 date "2014-02-18" @default.
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- W2036762805 title "Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG–SecDF–YajC–YidC" @default.
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- W2036762805 doi "https://doi.org/10.1073/pnas.1315901111" @default.
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