Effect of divalent cations on the ATPase activity ofEscherichia coliSecA
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(01)02265-7/fullpdf
Reference24 articles.
1. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
2. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
3. ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase
4. The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
5. Inhibition of Preprotein Translocation and Reversion of the Membrane Inserted State of SecA by a Carboxyl Terminus Binding MAb
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1. Stabilization of SecA ATPase by the primary cytoplasmic salt ofEscherichia coli;Protein Science;2019-05
2. Ca2+-induced stimulation of the membrane binding of Escherichia coli SecA and its association with signal peptides of secretory proteins;Archives of Biochemistry and Biophysics;2009-06
3. Selective Photoaffinity Labeling Identifies the Signal Peptide Binding Domain on SecA;Journal of Molecular Biology;2007-01
4. Structure and function of the bacterial Sec translocon (Review);Molecular Membrane Biology;2007-01
5. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase;The EMBO Journal;2003-09-01
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