Two Independent Mechanisms Down-regulate the Intrinsic SecA ATPase Activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli
2. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
3. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
4. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
5. ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase
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1. Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC;PLOS ONE;2017-06-02
2. Characterization of the minimal length of functional SecA in Escherichia coli;Biochemical and Biophysical Research Communications;2015-01
3. Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities;Biochemical and Biophysical Research Communications;2014-11
4. Phospholipids Induce Conformational Changes of SecA to Form Membrane-Specific Domains: AFM Structures and Implication on Protein-Conducting Channels;PLoS ONE;2013-08-16
5. Additional In Vitro and In Vivo Evidence for SecA Functioning as Dimers in the Membrane: Dissociation into Monomers Is Not Essential for Protein Translocation in Escherichia coli;Journal of Bacteriology;2008-02-15
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