The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1608, Issue 1, 2004, Pages 45-52

  Carneiro, Patrícia ^a   Duarte, Margarida ^a,b   Videira, Arnaldo ^a,b  

^a UNIVERSITY OF PORTO   (Portugal)

^b UNIVERSITY OF PORTO   (Portugal)

Author keywords

Gene expression; Mitochondrion; NADH dehydrogenase; Neurospora crassa; Respiratory mutant

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE;

ARTICLE; DNA SEQUENCE; FUNGUS GROWTH; GENE INACTIVATION; GENETIC TRANSCRIPTION; MITOCHONDRION; MUTANT; NEUROSPORA CRASSA; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

NEUROSPORA; NEUROSPORA CRASSA;

EID: 1642533556     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.10.004     Document Type: Article

References (46)

1. Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Ann. Rev. Biochem. 54:1985;1015-1069.
2. Moller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52:2001;561-591.
3. - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451:1999;157-161.
4. Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:1992;253-324.
5. Guenebaut V., Schlitt A., Weiss H., Leonard K., Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276:1998;105-112.
6. Videira A. Complex I from the fungus Neurospora crassa. Biochim. Biophys. Acta. 1364:1998;89-100.
7. Yagi T. The bacterial energy-transducing NADH-quinone oxidoreductases. Biochim. Biophys. Acta. 1141:1993;1-17.
8. Kerscher S.J. Diversity and origin of alternative NADH: ubiquinone oxidoreductases. Biochim. Biophys. Acta. 1459:2000;274-283.
9. Fang J., Beattie D.S. Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization. Biochemistry. 41:2002;3065-3072.
10. Videira A., Duarte M. From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta. 1555:2002;187-191.
11. Overkamp K.M., Bakker B.M., Kotter P., van Tuijl A., de Vries S., van Dijken J.P., Pronk J.T. In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J. Bacteriol. 182:2000;2823-2830.
12. Howitt C.A., Udall P.K., Vermaas W.F. Type 2 NADH dehydrogenases in the cyanobacterium Synechocystis sp. strain PCC 6803 are involved in regulation rather than respiration. J. Bacteriol. 181:1999;3994-4003.
13. Svensson A.S., Johansson F.I., Moller I.M., Rasmusson A.G. Cold stress decreases the capacity for respiratory NADH oxidation in potato leaves. FEBS Lett. 517:2002;79-82.
14. Svensson A.A., Rasmusson A.G. Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 28:2001;73-82.
15. Weiss H., von Jagow G., Klingenberg M., Buecher T. Characterization of Neurospora crassa mitochondria prepared with a grind-mill. Eur. J. Biochem. 14:1970;75-82.
16. Melo A.M., Duarte M., Moller I.M., Prokisch H., Dolan P.L., Pinto L., Nelson M.A., Videira A. The external calcium-dependent NADPH dehydrogenase from Neurospora crassa mitochondria. J. Biol. Chem. 276:2001;3947-3951.
17. Duarte M., Peters M., Schulte U., Videira A. The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria. Biochem. J. 371:2003;1005-1011.
18. Davis R.H., de Serres F.J. Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17A:1970;79-143.
19. Staben C., Jensen B., Singer M., Pollock J., Schechtman M., Kinsey J., Selker E.U. Use of a bacterial hygromycin B resistance gene as a dominant marker in Neurospora crassa transformation. Fungal Genet. Newslett. 36:1989;79-81.
20. Duarte M., Videira A. Respiratory chain complex I is essential for sexual development in Neurospora and binding of iron-sulfur clusters are required for enzyme assembly. Genetics. 156:2000;607-615.
21. Selker E.U. Premeiotic instability of repeated sequences in Neurospora crassa. Annu. Rev. Genet. 24:1990;579-613.
22. Videira A., Werner S. Assembly kinetics and identification of precursor proteins of complex I from Neurospora crassa. Eur. J. Biochem. 181:1989;493-502.
23. Sokolovsky V., Kaldenhoff R., Ricci M., Russo V.E.A. Fast and reliable miniprep RNA extraction from Neurospora crassa. Fungal Genet. Newslett. 37:1990;41.
24. Sambrook J., Russell D.W. Molecular Cloning: a Laboratory Manual. 2001;Cold Spring Harbor Laboratory Press, New York.
25. +)-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa. J. Mol. Biol. 329:2003;283-290.
26. Duarte M., Finel M., Videira A. Primary structure of a ferredoxin-like iron-sulfur subunit of complex I from Neurospora crassa. Biochim. Biophys. Acta. 1275:1996;151-153.
27. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
28. Zauner R., Christner J., Jung G., Borchart U., Machleidt W., Videira A., Werner S. Identification of the polypeptide encoded by the URF-1 gene of Neurospora crassa mtDNA. Eur. J. Biochem. 150:1985;447-454.
29. Towbin H., Staechelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354.
30. Melo A.M., Duarte M., Videira A. Primary structure and characterisation of a 64 kDa NADH dehydrogenase from the inner membrane of Neurospora crassa mitochondria. Biochim. Biophys. Acta. 1412:1999;282-287.
31. Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.U., Neupert W. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell. 53:1988;795-806.
32. Lill R., Stuart R.A., Drygas M.E., Nargang F.E., Neupert W. Import of cytochrome c heme lyase into mitochondria: a novel pathway into the intermembrane space. EMBO J. 11:1992;449-456.
33. Sollner T., Griffiths G., Pfaller R., Pfanner N., Neupert W. MOM19, an import receptor for mitochondrial precursor proteins. Cell. 59:1989;1061-1070.
34. Ferreirinha F., Duarte M., Melo A.M., Videira A. Effects of disrupting the 21 kDa subunit of complex I from Neurospora crassa. Biochem. J. 342:1999;551-554.
35. Fecke W., Sled V.D., Ohnishi T., Weiss H. Disruption of the gene encoding the NADH-binding subunit of NADH: ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3. Eur. J. Biochem. 220:1994;551-558.
36. da Silva M.V., Alves P.C., Duarte M., Mota N., Lobo-da-Cunha A., Harkness T.A., Nargang F.E., Videira A. Disruption of the nuclear gene encoding the 20.8-kDa subunit of NADH: ubiquinone reductase of Neurospora mitochondria. Mol. Gen. Genet. 252:1996;177-183.
37. Schwitzguebel J.P., Palmer J.M. Properties of mitochondria as a function of the growth stages of Neurospora crassa. J. Bacteriol. 149:1982;612-619.
38. Rasmusson A.G., Svensson S., Knoop V., Grohmann L., Brennicke A. Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: two enzymes are present in potato mitochondria. Plant J. 20:1999;79-87.
39. Fontaine E., Eriksson O., Ichas F., Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I. J. Biol. Chem. 273:1998;12662-12668.
40. Jung D.W., Bradshaw P.C., Pfeiffer D.R. Properties of a cyclosporin-insensitive permeability transition pore in yeast mitochondria. J. Biol. Chem. 272:1997;21104-21112.
41. Pahlman I.L., Larsson C., Averet N., Bunoust O., Boubekeur S., Gustafsson L., Rigoulet M. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J. Biol. Chem. 277:2002;27991-27995.
42. Schmit J.C., Brody S. Biochemical genetics of Neurospora crassa conidial germination. Bacteriol. Rev. 40:1976;1-41.
43. Watters M.K., Griffiths A.J. Tests of a cellular model for constant branch distribution in the filamentous fungus Neurospora crassa. Appl. Environ. Microbiol. 67:2001;1788-1792.
44. Sabar M., de Paepe R., de Kouchkovsky Y. Complex I impairment, respiratory compensations, and photosynthetic decrease in nuclear and mitochondrial male sterile mutants of Nicotiana sylvestris. Plant Physiol. 124:2000;1239-1250.
45. Barron J.T., Gu L., Parrillo J.E. Malate-aspartate shuttle, cytoplasmic NADH redox potential, and energetics in vascular smooth muscle. J. Mol. Cell Cardiol. 30:1998;1571-1579.
46. Eto K., Tsubamoto Y., Terauchi Y., Sugiyama T., Kishimoto T., Takahashi N., Yamauchi N., Kubota N., Murayama S., Aizawa T., Akanuma Y., Aizawa S., Kasai H., Yazaki Y., Kadowaki T. Role of NADH shuttle system in glucose-induced activation of mitochondrial metabolism and insulin secretion. Science. 283:1999;981-985.