PMID:9294424

Citation	Manting, EH, van der Does, C and Driessen, AJ (1997) In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase. J. Bacteriol. 179:5699-704
Abstract	Precursor protein translocation across the Escherichia coli inner membrane is mediated by the translocase, which is composed of a heterotrimeric integral membrane protein complex with SecY, SecE, and SecG as subunits and peripherally bound SecA. Cross-linking experiments were conducted to study which proteins are associated with SecA in vivo. Formaldehyde treatment of intact cells results in the specific cross-linking of SecA to SecY. Concurrently with the increased membrane association of SecA, an elevated amount of cross-linked product was obtained in cells harboring overproduced SecYEG complex. Cross-linked SecA copurified with hexahistidine-tagged SecY and not with SecE. The data indicate that SecA and SecY coexist as a stable complex in the cytoplasmic membrane in vivo.
Links	PubMed PMC179456
Keywords	Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Cross-Linking Reagents; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Transport Proteins; Molecular Weight; Recombinant Proteins
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