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Specification and Expression of Mitochondrial Cytochrome b

  • Henry R. Mahler

Abstract

Recent studies on the structure, organization, and expression of the mitochondrial gene for (apo)cytochrome b in Saccharomyces cerevisiae and related species have provided answers to some old questions and revealed some hitherto unexpected complexities of regulatory and, possibly, evolutionary significance.* To the first set belong, most importantly, the primary structure of the protein, a problem that had defied solution by protein sequencing techniques, but was solved by Nobrega and Tzagoloff (1980) by DNA sequencing: the polypeptide chain consists of 385 amino acids, corresponding to a molecular weight of 44,000. Another question that has been resolved without ambiguity concerns the type and number of polypeptides responsible for the multiplicity of cytochrome b species implicated in the b c 1 segment (Complex III, coenzyme QH2: cytochrome b oxidoreductase) of the mitochondrial respiratory (electron transfer) chain (reviewed by von Jagow and Sebald, 1980). Because single, defined, revertible mutational lesions in the coding segments of a unique and discrete gene, known as cob, are now known to result in the complete elimination or alteration of all forms of the cytochrome in question (Claisse et al., 1978; Mahler et al., 1978; Alexander et al., 1979; Haid et al., 1979; Kreike et al., 1979), all such cytochromes must have been synthesized with the same primary sequence. The different species observed may therefore be the consequence of placing the same polypeptide in different environments, of posttranslational modification, or a combination of these two effects. Related to this problem, and equally accessible by a combination of genetic and biochemical techniques, is the localization of sites of interaction between the polypeptide on the one hand, and heme or various characteristic inhibitors of Complex III (such as antimycin A, diuron, funiculosin and mucidin) on the other.

Keywords

Mitochondrial Genome Mitochondrial Gene Mitochondrial Cytochrome Schizosaccharomyces Pombe Discrete Gene 
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References

  1. Abelson, J. (1979). Annu. Rev. Biochem. 48, 1035–1069.CrossRefGoogle Scholar
  2. Alexander, N. J., Vincent, R. D., Perlman, P. S., Miller, D. H., Hanson, D. K., and Mahler, H. R. (1979). J. Biol. Chem. 254, 2471–2479.Google Scholar
  3. Alexander, N. J., Perlman, P. S., Hanson, D. K., and Mahler, H. R. (1980). Cell 20, 199–206.CrossRefGoogle Scholar
  4. Attardi, G., Cantatore, P., Ching, E., Crews, S., Gelfand, R., Merkel, C., Montoya, J., and Ojala, D. (1980). In The Organization and Expression of the Mitochondrial Genome (A. M. Kroon and C. Saccone, eds.), pp. 103–120, North-Holland, Amsterdam.Google Scholar
  5. Borst, P., and Grivell, L. A. (1978). Cell 15, 705–723.CrossRefGoogle Scholar
  6. Church, G. M., and Gilbert, W. (1980). In Mobilization and Reassembly of Genetic Information (D. R. Joseph, J. Schultz, W. A. Scott, and R. Werners, eds.), pp. 379–395, Academic Press, New York.Google Scholar
  7. Church, G. M., Slonimski, P. P., and Gilbert, W. (1979). Cell 18, 1209–1215.CrossRefGoogle Scholar
  8. Claisse, M. L., Spyridakis, A., Wambier-Kluppel, M. L., Pajot, P., and Slonimski, P. P. (1978). In Biochemistry and Genetics of Yeast (M. Bacila, B. L. Horecker, and A. O. M. Stoppani, eds.), pp. 369–390, Academic Press, New York.Google Scholar
  9. Claisse, M. L., Slonimski, P. P., Johnson, J., and Mahler, H. R. (1980). Mol. Gen. Genet. 177, 375–387.CrossRefGoogle Scholar
  10. Colson, A. M., and Slonimski, P. P. (1978). Mol. Gen. Genet. 167, 287–298.CrossRefGoogle Scholar
  11. Colson, A. M., Michaelis, G., Pratje, E., and Slonimski, P. P. (1979). Mol. Gen. Genet. 167, 299–300.CrossRefGoogle Scholar
  12. Craik, C. S., Buchman, S. B., and Beychok, S. (1980). Proc. Natl. Acad. Sci. USA 77, 1384–1388.CrossRefGoogle Scholar
  13. Crick, F. H. C. (1979). Science 204, 264–271.CrossRefGoogle Scholar
  14. Darnell, J. E., Jr. (1978). Science 202, 1257–1260.CrossRefGoogle Scholar
  15. Dhawale, S., Hanson, D. K., Alexander, N. J., Perlman, P. S., and Mahler, H. R. (1981). Proc. Natl. Acad. Sci. USA, 78, 1778–1782.CrossRefGoogle Scholar
  16. Dujon, B. (1979). Nature (London) 282, 777–778.CrossRefGoogle Scholar
  17. Gilbert, W. (1979). In Eucaryotic Gene Regulation (R. Axel, T. Maniatis, and C. F. Fox, eds.), pp. 1–12, Academic Press, New York.Google Scholar
  18. Grivell, L. A., Amberg, A. C., Hensgens, L. A. M., Roosendall, E., van Ommen, G.-J. B., and van Bruggen, E. F. J. (1980). In The Organization and Expression of the Mitochondria) Genome (A. M. Kroon and C. Saccone, eds.), pp. 37–50, North-Holland, Amsterdam.Google Scholar
  19. Haid, A., Schweyen, R. J., Bechmann, H., Kaudewitz, F., Solioz, M., and Schatz, G. (1979). Eur. J. Biochem. 94, 451–464.CrossRefGoogle Scholar
  20. Haid, A., Grosch, G., Schmelzer, C., Schweyen, R. S., and Kaudewitz, F. (1980). Curr. Genet. 1, 155–161.CrossRefGoogle Scholar
  21. Halbreich, A., Pajot, P., Foucher, M., Grandchamp, C., and Slonimski, P. P. (1980). Cell 19, 321–329.CrossRefGoogle Scholar
  22. Hanson, D. K., Miller, D. H., Mahler, H. R., Alexander, N. J., and Perlman, P. S. (1979). J. Biol. Chem. 254, 2480–2490.Google Scholar
  23. Jacq, C., Lazowska, J., and Slonimski, P. P. (1980). In The Organization and Expression of the Mitochondrial Genome (A. M. Kroon and C. Saccone, eds.), pp. 139–152, North-Holland, Amsterdam.Google Scholar
  24. Jacq, C., Lazowska, J., and Slonimski, P. P. (1980). In The Organization and Expression of the Mitochondrial Genome (A. M. Kroon and C. Saccone, eds.), pp. 139–152, North-Holland, Amsterdam.Google Scholar
  25. Kreike, J., Bechmann, H., Van Hemert, F. J., Schweyen, R. J., Boer, P. H., Kaudewitz, F., and Groot, G. S. P. (1979). Eur. J. Biochem. 101, 607–617.CrossRefGoogle Scholar
  26. Kroon, A. M., and Saccone, C. (eds.) (1980). The Organization and Expression of the Mitochondria) Genome, North-Holland, Amsterdam.Google Scholar
  27. Lamouroux, A., Pajot, P., Kochko, A., Halbreich, A., and Slonimski, P. P. (1980). In The Organization and Expression of the Mitochondrial Genome (A. M. Kroon and C. Saccone, eds.), pp. 139–152, North-Holland, Amsterdam.Google Scholar
  28. Lazowska, J., Jacq, C., and Slonimski, P. P. (1980). Cell 22, 333–348.CrossRefGoogle Scholar
  29. Lazowska, J., Jacq, C., and Slonimski, P. P. (1981). Cell 27, 12–14.CrossRefGoogle Scholar
  30. Lewin, B. (1980). Cell 22, 324–326.CrossRefGoogle Scholar
  31. Mahler, H. R. (1980). Ann. N.Y. Acad. Sci., 361, 53–75.CrossRefGoogle Scholar
  32. Mahler, H. R., and Perlman, P. S. (1971). Biochemistry 10, 2979–2990.CrossRefGoogle Scholar
  33. Mahler, H. R., and Perlman, P. S. (1979). In Extrachromosomal DNA (D. Cummings, P. Borst, I. Dawid, S. Weissman, and C. F. Fox, eds.), Vol. XV, pp. 11–33, Academic Press, New York.Google Scholar
  34. Mahler, H. R., and Raff, R. A. (1976). Int. Rev. Cytol. 43, 1–124.CrossRefGoogle Scholar
  35. Mahler, H. R., Hanson, D., Miller, D., Lin, C. C., Alexander, N. J., Vincent, R. D., and Perlman, P. S. (1978). In Biochemistry and Genetics of Yeasts (M. Bacila, B. Horecker, and A. O. M. Stoppani, eds.), pp. 513–547, Academic Press, New York.Google Scholar
  36. Mahler, H. R., Hanson, D., Miller, D., Lin, C. C., Alexander, N. J., Vincent, R. D., and Perlman, P. S. (1978). In Biochemistry and Genetics of Yeasts (M. Bacila, B. Horecker, and A. O. M. Stoppani, eds.), pp. 513–547, Academic Press, New York.Google Scholar
  37. Neupert, W., and Schatz, G. (1981). Trends in Biochemical Sciences 6, 1–4.CrossRefGoogle Scholar
  38. Nobrega, F. C., and Tzagoloff, A. (1980). J. Biol. Chem. 255, 9828–9837.Google Scholar
  39. Pajot, P., Wambier-Kluppel, M. L., and Slonimski, P. P. (1977). In Mitochondria 1977 (W. Bandlow, R. J. Schweyen, K. Wolf, and F. Kaudewitz, eds.), pp. 173–184, de Gruyter, Berlin.Google Scholar
  40. Perlman, P. S., Alexander, N. J., Hanson, D. K., and Mahler, H. R. (1980a). In Gene Structure and Expression (D. H. Dean, L. F. Johnson, P. C. Kimbal, and P. S. Perlman, eds.), pp. 210–253, Ohio State University, Columbus.Google Scholar
  41. Perlman, P. S., Mahler, H. R., Dhawale, S., Hanson, D., and Alexander, N. J. (1980b). in The Organization and Expression of the Mitochondrial Genome (A. M. Kroon and C. Saccone, eds.), pp. 161–172, North-Holland, Amsterdam.Google Scholar
  42. Roberts, H., Smith, C. C., Marzuki, S., and Linnane, W. A. (1980). Arch. Biochem. Biophys. 200, 387–395.CrossRefGoogle Scholar
  43. Schatz, G., and Mason, T. (1974). Annu. Rev. Biochem. 43, 51–87.CrossRefGoogle Scholar
  44. Schmelzer, C., Haid, A., Grosch, G., Schweyen, R. J., and Kaudewitz, F. (1981). J. Biol. Chem. 256, 7610–7619.Google Scholar
  45. Slonimski, P. P. (1980). C. R. Acad. Sci. 290, 331–334.Google Scholar
  46. Slonimski, P. P. (1980). C. R. Acad. Sci. 290, 331–334.Google Scholar
  47. Solioz, M., and Schatz, G. (1979). J. Biol. Chem. 254, 9331–9334.Google Scholar
  48. Tzagoloff, A., Macino, G., and Sebald, W. (1979). Annu. Rev. Biochem. 49, 419–441.CrossRefGoogle Scholar
  49. van Ommen, G.-J. B., Boer, P. H., Groot, G. S. P., de Haan, M., Roosendall, E., Grivell, L. A., Haid, A., and Schweyen, R. J. (1980). Cell 20, 172–183.Google Scholar
  50. von Jagow, G., and Sebald, W. (1980). Annu. Rev. Biochem. 49, 281–314.CrossRefGoogle Scholar
  51. Waring, R. B., Davies, R. W., Lee, S., Grisi, E., McPhail Berks, M., and Scazzocchio, C. (1981). Cell 27, 4–11.CrossRefGoogle Scholar
  52. Weiss, H., Wingfield, P., and Leonard, K. (1979). In Membrane Bioenergetics (C. P. Lee, G. Schatz, and L. Ernster, eds.), pp. 119–132, Addison—Wesley, Reading, Mass.Google Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Henry R. Mahler
    • 1
  1. 1.Department of Chemistry, and the Molecular, Cellular, and Developmental Biology ProgramIndiana UniversityBloomingtonUSA

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