Bacillus subtilis holo‐cytochrome c‐550 can be synthesised in aerobic Escherichia coli

FEBS Letters

von Wachenfeldt, Claes¹  Hederstedt, Lars¹ 

[1] Department of Microbiology, University of Lund, Sölvegatan 21, S-223 62 Lund, Sweden

关键词: phoA;    cccA;    Hemoprotein;    Cytochrome c biogenesis;    SDS;    sodium dodecyl sulfate;    kb;    kilobase(s);   

DOI  :  10.1016/0014-5793(90)81255-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown