SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

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

Cell

journal_title

Cell

authors

Economou A,Wickner W

doi

10.1016/s0092-8674(94)90582-7

subject

Has Abstract

pub_date

1994-09-09 00:00:00

pages

835-43

issue

5

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(94)90582-7

journal_volume

78

pub_type

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