Note. The nove nucleotide sequence data published here have been submitted to the GenBankTM/EMBL Data Bank and are available under accession numbers X88000 (S. tenacellus), X87997 (M. galopoda), X87998 (M. viridimarginata).
The Molecular Basis for the Natural Resistance of the Cytochrome bc1 Complex from Strobilurin-Producing Basidiomycetes to Center QP Inhibitors
Article first published online: 31 AUG 2004
European Journal of Biochemistry
Volume 235, Issue 1-2, pages 54–63, January 1996
How to Cite
Kraiczy, P., Haase, U., Gencic, S., Flindt, S., Anke, T., Brandt, U. and Von Jagow, G. (1996), The Molecular Basis for the Natural Resistance of the Cytochrome bc1 Complex from Strobilurin-Producing Basidiomycetes to Center QP Inhibitors. European Journal of Biochemistry, 235: 54–63. doi: 10.1111/j.1432-1033.1996.00054.x
- Issue published online: 31 AUG 2004
- Article first published online: 31 AUG 2004
- (Received 31 July 1995) – EJB 95 1263/6
- cytochrome b;
- natural resistance;
- exon/intron organization
Mitochondria from the strobilurin A producing basidiomycetes Strobilurus tenacellus and Mycena galopoda exhibit natural resistance to (E)-β-methoxyacrylate inhibitors of the ubiquinol oxidation center (center Qp) of the cytochrome bc1 complex. Isolated cytochrome bc1 complex from S. tenacellus was found to be highly similar to that of Saccharomyces cerevisiae with respect to subunit composition, as well as spectral characteristics and midpoint potentials of the heme centers.
To understand the molecular basis of natural resistance, we determined the exon/intron organization and deduced the sequences of cytochromes b from S. tenacellus, M. galopoda and a third basidiomycete, Mycena viridimarginata, which produces no strobilurin A. Comparative sequence analysis of two regions of cytochrome b known to contribute to the formation of center Qp suggested that the generally lower sensitivity of all three basidiomycetes was due to the replacement of a small amino acid residue in position 127 by isoleucine. For M. galopoda replacement of Gly143 by alanine and Gly153 by serine, for S. tenacellus replacement of a small residue in position 254 by glutamine and Asn261 by aspartate was found to be the likely causes for resistance to (E)-β-methoxyacrylates. The latler exchange is also found in Schizosaccharomyces pombe, which we found also to be naturally resistant to (E)-β-methoxyacrylates.