Synthetic Signal Peptides Specifically Recognize SecA and Stimulate ATPase Activity in the Absence of Preprotein
Open Access
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (19) , 11409-11412
- https://doi.org/10.1074/jbc.273.19.11409
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecABiochimica et Biophysica Acta (BBA) - Biomembranes, 1997
- Identification of a Region of Interaction between Escherichia coli SecA and SecY ProteinsPublished by Elsevier ,1997
- Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteinsProceedings of the National Academy of Sciences, 1997
- Escherichia coli Preprotein TranslocaseJournal of Biological Chemistry, 1996
- Signal peptides: exquisitely designed transport promotersMolecular Microbiology, 1994
- SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membraneMolecular Microbiology, 1993
- ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocaseCell, 1991
- The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membraneCell, 1990
- The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteinsCell, 1990
- Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptideJournal of Bacteriology, 1989