Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p

Barrie M Wilkinson, Yann Esnault, Rachel A Craven, Fabien Skiba, Jacques Fieschi, Francois Kepes, Colin J Stirling

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43 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)4549-4559
Number of pages11
JournalEMBO Journal
Volume16
Issue number15
DOIs
Publication statusPublished - 1997

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