Premium
Bacillus subtilis holo‐cytochrome c ‐550 can be synthesised in aerobic Escherichia coli
Author(s) -
von Wachenfeldt Claes,
Hederstedt Lars
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81255-m
Subject(s) - bacillus subtilis , cytochrome , cytochrome c , escherichia coli , cytochrome b , cytochrome p450 reductase , biochemistry , heme , biology , cytochrome c1 , cytochrome c peroxidase , coenzyme q – cytochrome c reductase , chemistry , gene , enzyme , bacteria , mitochondrion , genetics , mitochondrial dna
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 eytochrome c and suggests that eytochrome c ‐heme lyase activity is also present in aerobic E. coli . The membrane topology of B. subtilis eytochrome 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‐tenninal heme domain. A model for the organisation of B. subtilis cytochrome c ‐550 in the cytoplasmic membrane is presented.