Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein
(1999) In Journal of Bacteriology 181. p.685-688- Abstract
- The sequence of the N-terminal end of the deduced ctaC gene product of Bacillus species has the features of a bacterial lipoprotein. CtaC is the subunit II of cytochrome caa3, which is a cytochrome c oxidase. Using Bacillus subtilis mutants blocked in lipoprotein synthesis, we show that CtaC is a lipoprotein and that synthesis of the membrane-bound protein and covalent binding of heme to the cytochrome c domain is not dependent on processing at the N-terminal part of the protein. Mutants blocked in prolipoprotein diacylglyceryl transferase (Lgt) or signal peptidase type II (Lsp) are, however, deficient in cytochrome caa3 enzyme activity. Removal of the signal peptide from the CtaC polypeptide, but not lipid modification, is seemingly... (More)
- The sequence of the N-terminal end of the deduced ctaC gene product of Bacillus species has the features of a bacterial lipoprotein. CtaC is the subunit II of cytochrome caa3, which is a cytochrome c oxidase. Using Bacillus subtilis mutants blocked in lipoprotein synthesis, we show that CtaC is a lipoprotein and that synthesis of the membrane-bound protein and covalent binding of heme to the cytochrome c domain is not dependent on processing at the N-terminal part of the protein. Mutants blocked in prolipoprotein diacylglyceryl transferase (Lgt) or signal peptidase type II (Lsp) are, however, deficient in cytochrome caa3 enzyme activity. Removal of the signal peptide from the CtaC polypeptide, but not lipid modification, is seemingly required for formation of functional enzyme. (Less)
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- author
- Bengtsson, Jenny LU ; Tjalsma, Harold ; Rivolta, Carlo and Hederstedt, Lars LU
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Bacteriology
- volume
- 181
- pages
- 685 - 688
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:0032900982
- ISSN
- 0021-9193
- language
- English
- LU publication?
- yes
- id
- ea320c75-2bca-4655-8ae0-1f59c0f474ce
- date added to LUP
- 2017-07-18 09:47:33
- date last changed
- 2022-01-30 21:32:22
@article{ea320c75-2bca-4655-8ae0-1f59c0f474ce, abstract = {{The sequence of the N-terminal end of the deduced ctaC gene product of Bacillus species has the features of a bacterial lipoprotein. CtaC is the subunit II of cytochrome caa3, which is a cytochrome c oxidase. Using Bacillus subtilis mutants blocked in lipoprotein synthesis, we show that CtaC is a lipoprotein and that synthesis of the membrane-bound protein and covalent binding of heme to the cytochrome c domain is not dependent on processing at the N-terminal part of the protein. Mutants blocked in prolipoprotein diacylglyceryl transferase (Lgt) or signal peptidase type II (Lsp) are, however, deficient in cytochrome caa3 enzyme activity. Removal of the signal peptide from the CtaC polypeptide, but not lipid modification, is seemingly required for formation of functional enzyme.}}, author = {{Bengtsson, Jenny and Tjalsma, Harold and Rivolta, Carlo and Hederstedt, Lars}}, issn = {{0021-9193}}, language = {{eng}}, pages = {{685--688}}, publisher = {{American Society for Microbiology}}, series = {{Journal of Bacteriology}}, title = {{Subunit II of <em>Bacillus subtilis</em> cytochrome c oxidase is a lipoprotein}}, volume = {{181}}, year = {{1999}}, }