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- W2015320294 endingPage "4559" @default.
- W2015320294 startingPage "4549" @default.
- W2015320294 abstract "The heterotrimeric Sec61p complex is a key component of the protein translocation apparatus of the endoplasmic reticulum membrane. The complex characterized from yeast includes Sec61p, a 10-transmembrane-domain membrane protein which has a direct interaction with Sss1p, a small C-terminal anchor protein. In order to gain some insight into the architecture of this complex we have functionally expressed Sec61p as complementary N- and C-terminal fragments. Chemical crosslinking of Sss1p to specific Sec61p fragments in these functional combinations and suppression of sec61 mutants by over-expression of Sss1p have led to identification of the region which includes transmembrane domains TM6, TM7 and TM8 (amino acid residues L232-R406) of Sec61p as a major site of interaction with Sss1p." @default.
- W2015320294 created "2016-06-24" @default.
- W2015320294 creator A5010830567 @default.
- W2015320294 date "1997-08-01" @default.
- W2015320294 modified "2023-09-23" @default.
- W2015320294 title "Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p" @default.
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- W2015320294 doi "https://doi.org/10.1093/emboj/16.15.4549" @default.
- W2015320294 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1170081" @default.
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