Mitochondrialny gen cytochromu b [MTCYB]

• Autorzy: Knapik K , Jedrzejczak M. , Dybus A.

Warianty tytułu

EN

Cytochrome b [MTCYB] mitochondrial genome

• Języki publikacji: PL

Abstrakty

EN

A broad analysis of organisms is possible using molecular DNA as a marker. Mitochondrial genome and genes present in mtDNA, e.g. cytochrome b gene, are widely used in investigations and the significance of this research is becoming increasing. This gene is coded by heavy (H) strand of mtDNA. Cytochrome b is one of 11 subunits composed of bc1 complex of respiratory chain of mitochondria, the sequence of which is written down in the mitochondrial genome. Cytochrome b gene traits are a slow rate of variations during evolution, the presence of some parts of the gene that are more conserved and those which show high divergence rates. Those traits make the cytochrome b gene useful as a marker in many analyses. The cytochrome b gene is used as a tool in such studies as: legal and veterinary medicine, palaeontology, as well as phylogenetics, and it can attain the status of a universal metric.

Słowa kluczowe

PL

cytochrom b; DNA mitochondrialny; gen cytochromu b

• Wydawca: -
• Czasopismo: Medycyna Weterynaryjna
• Rocznik: 2006
• Tom: 62
• Numer: 11
• Opis fizyczny: s.1229-1232,rys.,bibliogr.

Twórcy

autor

Knapik K

• Akademia Rolnicza, ul.Doktora Judyma 12, 71-460 Szczecin

autor

Jedrzejczak M.

autor

Dybus A.

Bibliografia

• 1. Alves E., Óvilo C., Rodríguez M. C., Silió L.: Mitochondrial DNA sequence variation and phylogenetic relationships among Iberian pigs and other domestic and wild pig populations. Anim. Genet. 2003, 34, 319-324.
• 2. Anderson S., Bankier A. T., Barrell B. G., de Bruijn M. H. L., Coulson A. R., Drouin J., Eperon I. C., Nierlich D. P., Roe B. A., Sanger F., Schreier P. H., Smith A. J. H., Staden R., Young I. G.: Sequence and organization of the human mitochondrial genome. Nature 1981, 290, 457-465.
• 3. Andreu A. L., Hanna M. G., Reichmann H., Bruno C., Penn A. S., Tanji K., Pallotti F., Iwata S., Bonilla E., Lach B., Morgan-Hughes J., DiMauro S.: Exercise intolerance due to mutations in the cytochrome b gene of mitochondrial DNA. N. Engl. J. Med. 1999, 341, 1037-1044.
• 4. Brown M. D., Voljavec A. S., Lott M. T., Torroni A., Yang C.-C., Wallace D. C.: Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics 1992, 130, 163-173.
• 5. Budowle B., Allard M. W., Wilson M. R., Chakraborty R.: Forensics and mitochondrial DNA: Applications, debates, and foundations. Annu. Rev. Genomics Hum. Genet. 2003, 4, 119-141.
• 6. De Coo I. F. M., Renier W. O., Ruitenbeek W., Ter Laak H. J., Bakker M., Schagger H., Van Oost B. A., Smeets H. J. M.: A 4-base pair deletion in the mitochondrial cytochrome b gene associated with parkinsonism/MELAS overlap syndrome. Ann. Neurol. 1999, 45, 130-133.
• 7. Di Rago J. P., Colson A. M.: Molecular basis for resistance to antimycin and diuron, Q-cycle inhibitors acting at the Qi site in the mitochondrial ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae. J. Biol. Chem. 1988, 263, 12564-12570.
• 8. Drozd L., Karpiński M., Goleman M., Czyżowski P.: Charakterystyka krótkich fragmentów restrykcyjnych mtDNA u sarny (Capreolus capreolus) i jelenia szlachetnego (Cervus elaphus). Ann. Univ. Mariae Curie Sklodowska Sect. EE Zootech. 2003, 56, 23-30.
• 9. Edwards S. V., Arctander P., Wilson A. C.: Mitochondrial resolution of a deep branch in the genealogical tree for perching birds. Proc. Biol. Sci. 1991, 243, 99-107.
• 10. Esposti M. D., DeVries S., Crimi M., Ghelli A., Patarnello T., Meyer A.: Mitochondrial cytochrome b: evolution and structure of the protein. Biochim. Biophys. Acta 1993, 1143, 243-271.
• 11. Gubernator B., Króliczewski J., Rybka J., Szczepaniak A.: Białko Rieskiego - składnik transmembranowych kompleksów cytochromowych. Postêpy Biochem. 1997, 43, 41-50.
• 12. Hatefi Y., Haavik A. G., Griffiths D. E.: Studies on the Electron Transfer System XLI. Reduced Coenzyme Q-Cytochrome c Reductase. J. Biol. Chem. 1962, 237, 1681-1685.
• 13. Hauska G., Nitschke W., Herrmann R. G.: Amino acid identities in the three redox center-carrying polypeptides of cytochrome bc1/b6f complexes. J. Bioenerg. Biomembr. 1988, 20, 211-228.
• 14. Howell N.: Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis. J. Mol. Evol. 1989, 29, 157-169.
• 15. Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.: Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure Fold. Des. 2000, 8, 669-684.
• 16. Irwin D. M., Kocher T. D., Wilson A. C.: Evolution of the cytochrome b gene of mammals. Journal J. Mol. Evol. 1991, 32, 128-144.
• 17. Keightley J. A., Anitori R., Burton M. D., Quan F., Buist N. R. M., Kennaway N. G.: Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene. Am. J. Hum. Genet. 2000, 67, 1400-1410.
• 18. Kocher T. D., Thomas W. K., Meyer A., Edwarsds S. V., Paabo S., Villablanca F. X., Wilson A. C.: Dynamics of mitochondrial DNA evolution in animals: Amplification and sequencing with conserved primers. Proc. Natl. Acad. Sci. USA 1989, 86, 6196-6200.
• 19. Kvist L.: Phylogeny and phylogeography of European Parids. Acta Univ. Oul. A 2000, 341, 1-51.
• 20. Link T. A., Schagger H., von Jagow G.: Analysis of the structures of the subunits of the cytochrome bc1 complex from beef heart mitochondria. FEBS Lett. 1986, 204, 9-15.
• 21. Lubben M., Kolmerer B., Saraste M.: An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes. EMBO J. 1992, 11, 805-812.
• 22. Mancuso M., Filosto M., Stevens J. C., Patterson M., Shanske S., Krishna S., DiMauro S.: Mitochondrial myopathy and complex III deficiency in a patient with a new stop-codon mutation (G339X) in the cytochrome b gene. J. Neurol. Sci. 2003, 209, 61-63.
• 23. Matsunaga T., Chikuni K., Tanabeb R., Muroyab S., Shibata K., Yamada J., Shinmura Y.: A quick and simple method for the identification of meat species and meat products by PCR assay. Meat Sci. 1999, 51, 143-148.
• 24. Mitchell P.: Protonmotive redox mechanism of the cytochrome bc1 complex in the respiratory chain: protonmotive ubiquinone cycle. FEBS Lett. 1975, 56, 1-6.
• 25. Parson W., Pegoraro K., Niederstatter H., Foger M., Steinlechner M.: Species identification by means of the cytochrome b gene. Int. J. Legal Med. 2000, 114: 23-28.
• 26. Prusak B., Grzybowski T., Gralak M., Grzybowski G.: Przydatność analizy sekwencji genu cytochromu b mitochondrialnego DNA do określenia pochodzenia śladów biologicznych zwierząt i ludzi. Med. Weter. 2005, 61, 162-165.
• 27. Rieske J. S.: Composition, structure, and function of complex III of the respiratory chain. Biochim. Biophys. Acta 1976, 456, 195-247.
• 28. Romanowska E.: Kompleks cytochromów b/f z błon chloroplastowych. Postępy Biochem. 1994, 40, 59-63.
• 29. Saraste M.: Location of haem-binding sites in the mitochondrial cytochrome b. FEBS Letters 1984, 166, 367-372.
• 30. Saraste M.: Oxidative phosphorylation at the fin de siecle. Science 1999, 283, 1488-1493.
• 31. Soriano G. M., Ponamarev M. V., Carrell C. J., Xia D., Smith J. L., Cramer W. A.: Comparison of the cytochrome bc1 complex with the anticipated structure of the cytochrome b6f complex: Le plus ca change le plus c'est la meme chose. J. Bioenerg. Biomembr. 1999, 31, 201-213.
• 32. Trumpower B. L.: Cytochrome bc1 complexes of microorganisms. Microbiol. Rev. 1990, 54, 101-129.
• 33. Wallace D. C.: Mitochondrial DNA sequence variation in human evolution and disease. Proc. Natl. Acad. Sci. USA 1994, 91, 8739-8746.
• 34. Wallace D. C.: Mitochondrial diseases in man and mouse. Science 1999, 283, 1482-1488.
• 35. Widger W. R., Cramer W. A., Herrmann R. G., Trebst A.: Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6f-complex: Position of the cytochrome b hemes in the membrane. Proc. Natl. Acad. Sci. USA 1984, 81, 674-678.
• 36. Wikstrom M., Krab K., Saraste M.: Proton-translocating cytochrome complexes. Ann. Rev. Biochem. 1981, 50, 623-655.
• 37. Woese C. R.: Bacterial evolution. Microbiol. Rev. 1987, 51, 221-271.
• 38. Wolf C., Hübner P., Lüthy J.: Differentiation of sturgeon species by PCR-RFLP. Food Res. Intern. 1999, 32, 699-705.
• 39. Xia D., Yu C. A., Kim H., Xia J. Z., Kachurin A. M., Zhang L., Yu L., Deisenhofer J.: The Crystal Structure of the Cytochrome bc1 Complex from Bovine Heart Mitochondria. Science 1997, 277, 60-66.
• 40. Zawadzka M.: Systemy oceny minisatelitarnego polimorfizmu DNA i możliwości ich wykorzystania w hodowli zwierząt. Biotechnologia 2000, 4, 62-79.
• 41. Zhang Z., Huang L., Shulmeister V. M., Chi Y. I., Kim K. K., Hung L. W., Crofts A. R., Berry E. A., Kim S. H.: Electron transfer by domain movement in cytochrome bc1. Nature 1998, 392, 677-684.