Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein

Details

Serval ID
serval:BIB_A678D4C1402F
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein
Journal
Journal of Bacteriology
Author(s)
Bengtsson  J., Tjalsma  H., Rivolta  C., Hederstedt  L.
ISSN
0021-9193 (Print)
Publication state
Published
Issued date
01/1999
Peer-reviewed
Oui
Volume
181
Number
2
Pages
685-8
Notes
Journal Article Research Support, Non-U.S. Gov't --- Old month value: Jan
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.
Keywords
Amino Acid Sequence Aminolevulinic Acid/metabolism Bacillus subtilis/*enzymology/genetics Electron Transport Complex IV/*chemistry/*genetics/metabolism Escherichia coli/enzymology Lipoproteins/*chemistry/genetics/metabolism Macromolecular Substances *Membrane Proteins Molecular Sequence Data Palmitic Acid/metabolism Sequence Alignment Sequence Homology, Amino Acid Serine Endopeptidases/genetics/metabolism Transferases/genetics/metabolism
Pubmed
Web of science
Create date
24/01/2008 14:14
Last modification date
20/08/2019 15:11
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