Functional Signal Peptides Bind a Soluble N-terminal Fragment of SecA and Inhibit Its ATPase Activity
Open Access
- 1 June 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (22), 19648-19655
- https://doi.org/10.1074/jbc.m100098200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Synthetic Signal Peptides Specifically Recognize SecA and Stimulate ATPase Activity in the Absence of PreproteinPublished by Elsevier ,1998
- Biogenesis of the Gram-Negative Bacterial EnvelopeCell, 1997
- The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecABiochimica et Biophysica Acta (BBA) - Biomembranes, 1997
- The Amino-terminal Charge and Core Region Hydrophobicity Interdependently Contribute to the Function of Signal SequencesPublished by Elsevier ,1996
- Sec-dependent preprotein translocation in bacteriaArchiv für Mikrobiologie, 1996
- SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membraneMolecular Microbiology, 1993
- THE ENZYMOLOGY OF PROTEIN TRANSLOCATION ACROSS THE Escherichia coli PLASMA MEMBRANEAnnual Review of Biochemistry, 1991
- The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membraneCell, 1990
- Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.Proceedings of the National Academy of Sciences, 1989
- Signal sequencesBiochemistry, 1989