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- Title
Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p.
- Authors
Wilkinson, Barrie M.; Esnault, Yann; Craven, Rachel A.; Skiba, Fabien; Fieschi, Jacques; Képès, François; Stirling, Colin J.
- 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.
- Subjects
PROTEINS; ENDOPLASMIC reticulum; MEMBRANE proteins; CHROMOSOMAL translocation; GENETICS; CHEMICAL reactions; BIOCHEMISTRY
- Publication
EMBO Journal, 1997, Vol 16, Issue 15, p4549
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/16.15.4549