Abstract:
:Although the importance of interactions involving both the cytosolic and transmembrane regions of SecY and SecE has been documented, no information has been available for the physical contact sites of these translocase subunits in their cytosolic domains. We now carried out site-specific cross-linking experiments to identify SecY and SecE regions that are physically close. Cysteines introduced into SecY residue 244 in the fourth cytosolic domain (C4) as well as into residues 354-356 and 362 in the C5 domain could be cross-linked with natural or engineered residues at positions 79 and 81 in the central part of the cytosolic loop of SecE. These cross-linkages were abolished by the Gly240 mutation in the SecY C4 region as well as by prlG alterations in SecE transmembrane segment 3, known to compromise SecY-SecE interaction. We suggest that the cytosolic and intramembrane interactions bring these two subunits together, forming a functionally crucial SecYE interface involving the SecY C5 region and the conserved cytosolic segment of SecE.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Satoh Y,Mori H,Ito Kdoi
10.1021/bi034333vsubject
Has Abstractpub_date
2003-06-24 00:00:00pages
7442-7issue
24eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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