CtaG is required for formation of active cytochrome C oxidase in Bacillus subtilis
(2004) In Microbiology 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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https://lup.lub.lu.se/record/288230
- author
- Bengtsson, Jenny ; von Wachenfeldt, Claes LU ; Winstedt, Lena LU ; Nygaard, Per and Hederstedt, Lars LU
- organization
- publishing date
- 2004
- 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
- Microbiology
- 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
- 2016-04-01 12:37:42
- date last changed
- 2024-01-09 03:14:15
@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}}, keywords = {{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 = {{Microbiology}}, 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}}, doi = {{10.1099/mic.0.26691-0}}, volume = {{150}}, year = {{2004}}, }