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CtaG is required for formation of active cytochrome C oxidase in Bacillus subtilis

Bengtsson, Jenny; von Wachenfeldt, Claes LU ; Winstedt, Lena LU ; Nygaard, Per and Hederstedt, Lars LU (2004) In Microbiology1994-01-01+01:00 150. p.415-425
Abstract
The Gram-positive bacterium Bacillus subtilis contains two respiratory oxidases of the haem-copper superfamily: cytochrome aa(3), which is a quinol oxidase, and cytochrome caa(3), which is a cytochrome c oxidase. Cytochrome c oxidase uniquely contains a di-copper centre, Cu-A. B. subtilis CtaG is a membrane protein encoded by the same gene cluster as that which encodes the subunits of cytochrome c oxidase. The role of B. subtilis CrtaG and orthologous proteins present in many other Gram-positive bacteria has remained unexplored. The sequence of CtaG is unrelated to that of CtaG/Cox11p, of proteobacteria and eukaryotic cells. This study shows that B. subtilis CtaG is essential for the formation of active cytochrome caa(3) but is not... (More)
The Gram-positive bacterium Bacillus subtilis contains two respiratory oxidases of the haem-copper superfamily: cytochrome aa(3), which is a quinol oxidase, and cytochrome caa(3), which is a cytochrome c oxidase. Cytochrome c oxidase uniquely contains a di-copper centre, Cu-A. B. subtilis CtaG is a membrane protein encoded by the same gene cluster as that which encodes the subunits of cytochrome c oxidase. The role of B. subtilis CrtaG and orthologous proteins present in many other Gram-positive bacteria has remained unexplored. The sequence of CtaG is unrelated to that of CtaG/Cox11p, of proteobacteria and eukaryotic cells. This study shows that B. subtilis CtaG is essential for the formation of active cytochrome caa(3) but is not required for assembly of the core subunits I and II with haem in the membrane and it has no role in the synthesis of active cytochrome aa(3). B. subtilis YpmQ, a homologue to Sco1p of eukaryotic cells, is also a membrane-bound cytochrome c oxidase-specific assembly factor. Properties of CtaG- and YpmQ-deficient mutants were compared. Cells lacking YpmQ showed a low cytochrome c oxidase activity and this defect was suppressed by the supplementation of the growth medium with copper ions. It has previously been proposed that YpmQ/Sco1p is involved in synthesis of the Cu-A centre. The results of this study are consistent with this proposal but the exact role of YpmQ in assembly of cytochrome c oxidase remains to be elucidated. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
TMPD, N,N,N′N′-tetramethyl-p-phenylenediamine, ICP-MS, inductively coupled plasma emission mass spectroscopy
in
Microbiology1994-01-01+01:00
volume
150
pages
415 - 425
publisher
MAIK Nauka/Interperiodica
external identifiers
  • pmid:14766920
  • wos:000188841500020
  • scopus:1242273761
ISSN
1465-2080
DOI
10.1099/mic.0.26691-0
language
English
LU publication?
yes
id
2344232f-ef70-4523-bb2f-ee94b55c28a0 (old id 288230)
date added to LUP
2007-10-17 08:15:16
date last changed
2017-08-10 10:06:10
@article{2344232f-ef70-4523-bb2f-ee94b55c28a0,
  abstract     = {The Gram-positive bacterium Bacillus subtilis contains two respiratory oxidases of the haem-copper superfamily: cytochrome aa(3), which is a quinol oxidase, and cytochrome caa(3), which is a cytochrome c oxidase. Cytochrome c oxidase uniquely contains a di-copper centre, Cu-A. B. subtilis CtaG is a membrane protein encoded by the same gene cluster as that which encodes the subunits of cytochrome c oxidase. The role of B. subtilis CrtaG and orthologous proteins present in many other Gram-positive bacteria has remained unexplored. The sequence of CtaG is unrelated to that of CtaG/Cox11p, of proteobacteria and eukaryotic cells. This study shows that B. subtilis CtaG is essential for the formation of active cytochrome caa(3) but is not required for assembly of the core subunits I and II with haem in the membrane and it has no role in the synthesis of active cytochrome aa(3). B. subtilis YpmQ, a homologue to Sco1p of eukaryotic cells, is also a membrane-bound cytochrome c oxidase-specific assembly factor. Properties of CtaG- and YpmQ-deficient mutants were compared. Cells lacking YpmQ showed a low cytochrome c oxidase activity and this defect was suppressed by the supplementation of the growth medium with copper ions. It has previously been proposed that YpmQ/Sco1p is involved in synthesis of the Cu-A centre. The results of this study are consistent with this proposal but the exact role of YpmQ in assembly of cytochrome c oxidase remains to be elucidated.},
  author       = {Bengtsson, Jenny and von Wachenfeldt, Claes and Winstedt, Lena and Nygaard, Per and Hederstedt, Lars},
  issn         = {1465-2080},
  keyword      = { TMPD,N,N,N′N′-tetramethyl-p-phenylenediamine,ICP-MS,inductively coupled plasma emission mass spectroscopy},
  language     = {eng},
  pages        = {415--425},
  publisher    = {MAIK Nauka/Interperiodica},
  series       = {Microbiology1994-01-01+01:00},
  title        = {CtaG is required for formation of active cytochrome C oxidase in <em>Bacillus subtilis</em>},
  url          = {http://dx.doi.org/10.1099/mic.0.26691-0},
  volume       = {150},
  year         = {2004},
}