Summary
Two cytochrome b respiratory—deficient mutants were sequenced and their DNA base change identified, leading to the replacement of glycine (G137 by valine or glutamicacid. No variation in their cytochrome b content with regard to cytochrome oxidase and cytochrome (c+c1) was found to have occurred. Their cellular respiratory activity with various substrates was partly conserved and was totally inhibited by antimycin A. Their ubiquinol (QH2)-cytochrome c reductase/mole cytochrome b activity decreased by about 50%. Paradoxically their growth on respiratory substrate was abolished. Both mutants retained a high-affinity binding site for antimycin A, and exhibited a myxothiazol—resistance at the mitochondrial level. It seems likely that the mutated position (137), which belongs to the ubiquinol oxidizing domain of the bc1 complex, interferes, directly or indirectly, with the respiratory growth capacity of the cell.
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References
Berden JA, Slater EC (1972) Biochim Biophys Acta 256:199–215
Brasseur R (1988) J Biol Chem 263:12564–12570
Chevillotte-Brivet P, Meunier-Lemesle D (1980) Eur J Biochem 111:161–169
Chevillotte-Brivet P, Meunier-Lemesle D, Forget N, Pajot P (1983) Eur J Biochem 129:653–661
Chevillotte-Brivet P, Salou G, Forget N, Meunier-Lemesle D (1987a) Biochimie 69:25–36
Chevillotte-Brivet P, Salou G, Meunier-Lemesle D (1987 b) Current Genet 12:111–117
Crofts A, Robinson H, Andrews K, Van Doren S, Berry E (1987) In: Papa S, Chance B, Ernster L (eds) Cytochrome systems, pp 617–624
di Rago J-P, Colson A-M (1988) J Biol Chem 263:12564–12570
di Rago J-P, Coppée J-Y, Colson A-M (1989) J Biol Chem 264:14543–14548
di Rago J-P, Netter P, Slonimski PP (1990a) J Biol Chem 265:3332–3339
di Rago J-P, Netter P, Slonimski PP (1990 b) J Biol Chem (in press)
Haid A, Schweyen RJ, Belmmann M, Kaudewitz F, Solioz M, Schatz G (1979) Eur J Biochem 94:451–464
Hauska G, Hurt E, Gabellini N, Lockau W (1983) Biochim Biophys Acta 726:97–133
Hauska G, Nitshke W, Herrmann RG (1988) J Bioenerg Biomembr 20:211–217
Jacq C, Lazowska J, Slonimski PP (1980) In: Kroon AM, Saccone C (eds) The organisation and expression of the mitochondrial genome. North-Holland, Amsterdam, pp 139–152
Kotylak Z, Slonimski PP (1977) In: Bandlow W, Schweyen RJ, Wolf K, Kaudewitz F (eds) Mitochondria 1977, Proc Collq Genet, Biogenesis of mitochondria. de Gruyter, Berlin, pp 162–172
Lowry OM, Rosebrought NJ, Farr AL, Randall RJ (1951) J Biol Chem 193:265–275
Meunier-Lemesle D, Chevillotte-Brivet P, Pajot P (1980) Eur J Biochem 111:151–160
Mitchell P (1976) J Theor Biol 62:327–367
Rao JK, Argos P (1986) Biochim Biophys Acta 869:197–205
Rich P (1984) Biochim Biophys Acta 768:53–79
von Jagow G, Ljungdahl PO, Graf PO, Onhishi T, Trumpower BL (1983) J Biol Chem 259:6318–6326
Wikström M, Krab K (1986) J Bioenerg Biomembr 18:181–193
Yang X, Trumpower BL (1988) J Biol Chem 263:11962–11970
Yang X, Ljungdahl PO, Payne WE, Trumpower BL (1987) In: Osawa T, Papa S (eds) Bioenergetics: structure and function in energy transducing systems. Japan Sci Soc Press Tokyo/ Springer-Verlag, Berlin, pp 63–70
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Communicated by P. P. Slonimski
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Tron, T., Lemesle-Meunier, D. Two substitutions at the same position in the mitochondrial cytochrome b gene of S. cerevisiae induce a mitochondrial myxothiazol resistance and impair the respiratory growth of the mutated strains abbeit maintaining a good electron transfer activity. Curr Genet 18, 413–419 (1990). https://doi.org/10.1007/BF00309910
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DOI: https://doi.org/10.1007/BF00309910