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Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein

Bengtsson, Jenny LU ; Tjalsma, Harold; Rivolta, Carlo and Hederstedt, Lars LU (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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publication status
published
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in
Journal of Bacteriology
volume
181
pages
685 - 688
publisher
American Society for Microbiology
ISSN
0021-9193
language
English
LU publication?
yes
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ea320c75-2bca-4655-8ae0-1f59c0f474ce
date added to LUP
2017-07-18 09:47:33
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2017-08-11 12:01:09
@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},
}