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Haem-delivery proteins in cytochrome c maturation System II

Ahuja, Umesh; Kjelgaard, Peter LU ; Schulz, Benjamin L.; Thoeny-Meyer, Linda and Hederstedt, Lars LU (2009) In Molecular Microbiology 73(6). p.1058-1071
Abstract
P>Cytochromes of the c-type function on the outer side of the cytoplasmic membrane in bacteria where they also are assembled from apo-cytochrome polypeptide and haem. Two distinctly different systems for cytochrome c maturation are found in bacteria. System I present in Escherichia coli has eight to nine different Ccm proteins. System II is found in Bacillus subtilis and comprises four proteins: CcdA, ResA, ResB and ResC. ResB and ResC are poorly understood polytopic membrane proteins required for cytochrome c synthesis. We have analysed these two B. subtilis proteins produced in E. coli and in the native organism. ResB is shown to bind protohaem IX and haem is found covalently bound to residue Cys-138. Results in B. subtilis suggest... (More)
P>Cytochromes of the c-type function on the outer side of the cytoplasmic membrane in bacteria where they also are assembled from apo-cytochrome polypeptide and haem. Two distinctly different systems for cytochrome c maturation are found in bacteria. System I present in Escherichia coli has eight to nine different Ccm proteins. System II is found in Bacillus subtilis and comprises four proteins: CcdA, ResA, ResB and ResC. ResB and ResC are poorly understood polytopic membrane proteins required for cytochrome c synthesis. We have analysed these two B. subtilis proteins produced in E. coli and in the native organism. ResB is shown to bind protohaem IX and haem is found covalently bound to residue Cys-138. Results in B. subtilis suggest that also ResC can bind haem. Our results complement recent findings made with Helicobacter CcsBA supporting the hypothesis that ResBC as a complex translocates haem by attaching it to ResB on the cytoplasmic side of the membrane and then transferring it to an extra-cytoplasmic location in ResC, from where it is made available to the apo-cytochromes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
73
issue
6
pages
1058 - 1071
publisher
Wiley-Blackwell
external identifiers
  • wos:000269809000009
  • scopus:70350150776
ISSN
1365-2958
DOI
10.1111/j.1365-2958.2009.06833.x
language
English
LU publication?
yes
id
815bec6e-f041-4a03-bd28-a8c0e96b5305 (old id 1492267)
date added to LUP
2009-10-16 17:01:51
date last changed
2017-01-01 04:25:02
@article{815bec6e-f041-4a03-bd28-a8c0e96b5305,
  abstract     = {P>Cytochromes of the c-type function on the outer side of the cytoplasmic membrane in bacteria where they also are assembled from apo-cytochrome polypeptide and haem. Two distinctly different systems for cytochrome c maturation are found in bacteria. System I present in Escherichia coli has eight to nine different Ccm proteins. System II is found in Bacillus subtilis and comprises four proteins: CcdA, ResA, ResB and ResC. ResB and ResC are poorly understood polytopic membrane proteins required for cytochrome c synthesis. We have analysed these two B. subtilis proteins produced in E. coli and in the native organism. ResB is shown to bind protohaem IX and haem is found covalently bound to residue Cys-138. Results in B. subtilis suggest that also ResC can bind haem. Our results complement recent findings made with Helicobacter CcsBA supporting the hypothesis that ResBC as a complex translocates haem by attaching it to ResB on the cytoplasmic side of the membrane and then transferring it to an extra-cytoplasmic location in ResC, from where it is made available to the apo-cytochromes.},
  author       = {Ahuja, Umesh and Kjelgaard, Peter and Schulz, Benjamin L. and Thoeny-Meyer, Linda and Hederstedt, Lars},
  issn         = {1365-2958},
  language     = {eng},
  number       = {6},
  pages        = {1058--1071},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Haem-delivery proteins in cytochrome c maturation System II},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.2009.06833.x},
  volume       = {73},
  year         = {2009},
}