Direct Demonstration of ATP-dependent Release of SecA from a Translocating Preprotein by Surface Plasmon Resonance
Open Access
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (32) , 29581-29586
- https://doi.org/10.1074/jbc.m303490200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Membrane Topology Inversion of SecG Detected by Labeling with a Membrane-Impermeable Sulfhydryl Reagent that Causes a Close Association of SecG with SecAThe Journal of Biochemistry, 2002
- The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structureThe EMBO Journal, 2002
- Escherichia coli translocase: the unravelling of a molecular machineMolecular Microbiology, 2000
- SecYEG assembles into a tetramer to form the active protein translocation channelThe EMBO Journal, 2000
- Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzymeThe EMBO Journal, 1997
- Identification of a Region of Interaction between Escherichia coli SecA and SecY ProteinsPublished by Elsevier ,1997
- SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimerBiochemistry, 1993
- SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimerBiochemical and Biophysical Research Communications, 1991
- The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocationCell, 1990
- SecA protein is required for secretory protein translocation into E. coli membrane vesiclesCell, 1988