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Bacillus subtilis holo-cytochrome c-550 can be synthesized in aerobic Escherichia coli

von Wachenfeldt, Claes LU and Hederstedt, Lars LU (1990) In FEBS Letters 270(1-2). p.147-151
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 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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
phoA, cccA, Hemoprotein, Cytochrome c biogenesis, SDS, sodium dodecyl sulfate
in
FEBS Letters
volume
270
issue
1-2
pages
147 - 151
publisher
Wiley-Blackwell
external identifiers
  • scopus:0025002908
ISSN
1873-3468
DOI
10.1016/0014-5793(90)81255-M
language
English
LU publication?
yes
id
d5d0bba8-690d-4fa7-bd6f-4e7522f5ce40
date added to LUP
2017-07-18 10:40:38
date last changed
2017-11-05 05:20:36
@article{d5d0bba8-690d-4fa7-bd6f-4e7522f5ce40,
  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 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.},
  author       = {von Wachenfeldt, Claes and Hederstedt, Lars},
  issn         = {1873-3468},
  keyword      = {phoA,cccA,Hemoprotein,Cytochrome c biogenesis,SDS,sodium dodecyl sulfate},
  language     = {eng},
  number       = {1-2},
  pages        = {147--151},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {<em>Bacillus subtilis</em> holo-cytochrome c-550 can be synthesized in aerobic <em>Escherichia coli</em>},
  url          = {http://dx.doi.org/10.1016/0014-5793(90)81255-M},
  volume       = {270},
  year         = {1990},
}