| 1. |
- Bengtsson, Jenny, et al.
(författare)
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Bacillus subtilis contains two small c-type cytochromes with homologous heme-domains but different types of membrane-anchors
- 1999
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Ingår i: Journal of Biological Chemistry. - : Elsevier BV. - 1083-351X .- 0021-9258. ; 274, s. 26179-26184
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Tidskriftsartikel (refereegranskat)abstract
- We demonstrate that the cccB gene, identified in the Bacillus subtilis genome sequence project, is the structural gene for a 10-kDa membrane-bound cytochrome c551 lipoprotein described for the first time in B. subtilis. Apparently, CccB corresponds to cytochrome c551 of the thermophilic bacterium Bacillus PS3. The heme domain of B. subtilis cytochrome c551 is very similar to that of cytochrome c550, a protein encoded by the cccA gene and anchored to the membrane by a single transmembrane polypeptide segment. Thus, B. subtilis contains two small, very similar, c-type cytochromes with different types of membrane anchors. The cccB gene is cotranscribed with the yvjA gene, and transcription is repressed by glucose. Mutants deleted for cccB or yvjA-cccB show no apparent growth, sporulation, or germination defect. YvjA is not required for the synthesis of cytochrome c551, and its function remains unknown.
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| 2. |
- Bengtsson, Jenny, et al.
(författare)
-
Subunit II of Bacillus subtilis cytochrome c oxidase is a lipoprotein
- 1999
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Ingår i: Journal of Bacteriology. - 0021-9193. ; 181, s. 685-688
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Tidskriftsartikel (refereegranskat)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.
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