In Vivo Membrane Topology of Escherichia coli SecA ATPase Reveals Extensive Periplasmic Exposure of Multiple Functionally Important Domains Clustering on One Face of SecA*
Jilaveanu LB, Oliver DB. In Vivo Membrane Topology of Escherichia coli SecA ATPase Reveals Extensive Periplasmic Exposure of Multiple Functionally Important Domains Clustering on One Face of SecA*. Journal Of Biological Chemistry 2006, 282: 4661-4668. PMID: 17166834, DOI: 10.1074/jbc.m610828200.Peer-Reviewed Original ResearchConceptsSecA ATPaseEscherichia coli SecA ATPaseProtein translocation pathwayProtein-conducting channelRegion of SecABacterial plasma membraneMembrane-integrated stateTransport of proteinsSecA mutantSecA domainProtein translocationMembrane topologyMembrane cyclingSecA structureMembrane insertionTranslocation pathwayProtein cargoPlasma membraneSulfhydryl labelingN-domainSecAC-domainTrans sideChannel complexLabeling patternsSecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation
Jilaveanu LB, Oliver D. SecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation. Journal Of Bacteriology 2006, 188: 335-338. PMID: 16352850, PMCID: PMC1317605, DOI: 10.1128/jb.188.1.335-338.2006.Peer-Reviewed Original Research