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Journal of Bacteriology, January 1999, p. 685-688, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Subunit II of Bacillus subtilis Cytochrome c Oxidase Is a Lipoprotein

Jenny Bengtsson,1 Harold Tjalsma,2 Carlo Rivolta,3 and Lars Hederstedt1,*

Department of Microbiology, Lund University, Lund, Sweden1; Department of Genetics, University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute, Groningen, The Netherlands2; and Institut de Génétique et de Biologie Microbiennes, Université de Lausanne, Lausanne, Switzerland3

Received 10 September 1998/Accepted 30 October 1998

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.

* Corresponding author. Mailing address: Department of Microbiology, Lund University, Sölvegatan 12, S-223 62 Lund, Sweden. Phone: 46 (46) 2228622. Fax: 46 (46) 157839. E-mail: Lars.Hederstedt{at}mikrbiol.lu.se.

Journal of Bacteriology, January 1999, p. 685-688, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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