Premium
Biochemical characterization of the presecretory protein translocation machinery of Escherichia coli
Author(s) -
Tokuda Hajime
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00317-3
Subject(s) - chromosomal translocation , escherichia coli , cytoplasm , microbiology and biotechnology , biology , vesicle , transport protein , membrane protein , biochemistry , membrane transport protein , chemiosmosis , biophysics , membrane , chemistry , enzyme , gene , atp synthase
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.