Abstract:
:SecA, the peripheral subunit of E. coli preprotein translocase, alternates between a membrane inserted and a deinserted state as part of the catalytic cycle of preprotein translocation. When SecA is complexed with SecY/E and preprotein, ATP drives a profound conformational change, leading to membrane insertion of a 30 kDa domain of SecA. The inserted domain is protease-inaccessible from the cytosolic side of the membrane, but becomes accessible upon membrane disruption. Concomitant with 30 kDa domain insertion, approximately 20 aminoacyl residues of the preprotein are translocated. Additional ATP, which may be hydrolyzed at the second ATP site of SecA, releases the translocated preprotein and allows the 30 kDa domain to deinsert, whence it can exchange with cytosolic SecA. Thus, SecA is the mobile subunit of an integral membrane transporter, consuming ATP during both the insertion and deinsertion phases of its catalytic cycle while guiding preprotein segments across the membrane.
journal_name
Celljournal_title
Cellauthors
Economou A,Wickner Wdoi
10.1016/s0092-8674(94)90582-7subject
Has Abstractpub_date
1994-09-09 00:00:00pages
835-43issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(94)90582-7journal_volume
78pub_type
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