Sec translocon has an insertase-like function in addition to polypeptide conduction through the channel [version 1; peer review: 4 approved]

The Sec translocon provides a polypeptide-conducting channel, which is insulated from the hydrophobic lipidic environment of the membrane, for translocation of hydrophilic passenger polypeptides. Its lateral gate allows a downstream hydrophobic segment (stop-transfer sequence) to exit the channel la...

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Published inF1000 research Vol. 8; p. 2126
Main Authors Ito, Koreaki, Shimokawa-Chiba, Naomi, Chiba, Shinobu
Format Journal Article
LanguageEnglish
Published England Faculty of 1000 Ltd 2019
F1000 Research Limited
F1000 Research Ltd
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Summary:The Sec translocon provides a polypeptide-conducting channel, which is insulated from the hydrophobic lipidic environment of the membrane, for translocation of hydrophilic passenger polypeptides. Its lateral gate allows a downstream hydrophobic segment (stop-transfer sequence) to exit the channel laterally for integration into the lipid phase. We note that this channel model only partly accounts for the translocon function. The other essential role of translocon is to facilitate de novo insertion of the N-terminal topogenic segment of a substrate polypeptide into the membrane. Recent structural studies suggest that de novo insertion does not use the polypeptide-conducting channel; instead, it takes place directly at the lateral gate, which is prone to opening. We propose that the de novo insertion process, in concept, is similar to that of insertases (such as YidC in bacteria and EMC3 in eukaryotes), in which an intramembrane surface of the machinery provides the halfway point of insertion.
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No competing interests were disclosed.
ISSN:2046-1402
2046-1402
DOI:10.12688/f1000research.21065.1