title: Bacillus subtilis holo-cytochrome c-550 can be synthesised in aerobic Escherichia coli.
abstract: Bacillus subtilis membrane-bound holo-cytochrome c-550 was found to be expressed from the structural gene cloned on a plasmid vector in aerobically grown Escherichia coli and exhibited normal biochemical properties. This occurs despite the lack of endogenous cytochrome c and suggests that cytochrome c-heme lyase activity is also present in aerobic E. coli. The membrane topology of B. subtilis cytochrome c-550 was studied using fusions to alkaline phosphatase (PhoA). The results show that the heme domain (at least when fused to PhoA) can be translocated as apo-cytochrome and confirm that the N-terminal part of the cytochrome functions as both export signal and membrane anchor for the C-terminal heme domain. A model for the organisation of B. subtilis cytochrome c-550 in the cytoplasmic membrane is presented.
authors.affiliation: Department of Microbiology, University of Lund, Sweden.
authors.forename: C
authors.initials: C
authors.lastname: von Wachenfeldt
authors.forename: L
authors.initials: L
authors.lastname: Hederstedt
mesh_terms: D000469:Alkaline Phosphatase / Q000096:biosynthesis; D001412:Bacillus subtilis / Q000201:enzymology*; D001420:Bacteria, Aerobic / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D003574:Cytochrome c Group / Q000096:biosynthesis* / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D008958:Models, Molecular; D010455:Peptides / Q000502:physiology; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D013329:Structure-Activity Relationship
chemical_list: D003574:Cytochrome c Group; D010455:Peptides; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D006418:Heme; C031732:cytochrome C-550; D000469:Alkaline Phosphatase