Biochemical characterization of the presecretory protein translocation machinery of Escherichia coli.

Abstract:

:The protein translocation apparatus in Escherichia coli has been studied both genetically and biochemically. In vitro protein translocation systems involving everted membrane vesicles or reconstituted proteoliposomes have significantly contributed to biochemical clarification of the structure, mechanism and energetics of the apparatus. It is established that SecA, SecY and SecE are essential components, and play fundamental roles in the translocation reaction, and that both ATP and a proton motive force are required for the translocation. A new membrane factor, SecG, was found to participate in the formation of the apparatus, causing significant enhancement of the activity. SecD was found to play a role in the release of translocated proteins from the outer surface of the cytoplasmic membrane.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Tokuda H

doi

10.1016/0014-5793(94)00317-3

subject

Has Abstract

pub_date

1994-06-06 00:00:00

pages

65-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)00317-3

journal_volume

346

pub_type

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