Bacillus subtilis holo-cytochrome c-550 can be synthesized in aerobic Escherichia coli
(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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https://lup.lub.lu.se/record/d5d0bba8-690d-4fa7-bd6f-4e7522f5ce40
- author
- von Wachenfeldt, Claes LU and Hederstedt, Lars LU
- organization
- publishing date
- 1990
- 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
- 2024-01-14 00:52:26
@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}}, keywords = {{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}}, doi = {{10.1016/0014-5793(90)81255-M}}, volume = {{270}}, year = {{1990}}, }