Subunit composition of mitochondrial complex I from the yeast Yarrowia lipolytica

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1658, Issue 1-2, 2004, Pages 148-156

  Abdrakhmanova, Albina ^a   Zickermann, Volker ^a   Bostina, Mihnea ^b   Radermacher, Michael ^c   Schägger, Hermann ^a   Kerscher, Stefan ^a   Brandt, Ulrich ^a  

^a GOETHE UNIVERSITY MEDICAL SCHOOL   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^c UNIVERSITY OF VERMONT   (United States)

Author keywords

Accessory subunit; Complex I; doubled sodium dodecylsulfate polyacrylamide gel electrophoresis; dSDS PAGE; LDAO; MALDI; Mass spectrometry; N lauryl N,N dimethylamine N oxide; NADH:ubiquinone oxidoreductase; Yarrowia lipolytica

Indexed keywords

MONOCLONAL ANTIBODY; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCROSE;

ANTIBODY SPECIFICITY; CENTRIFUGATION; ELECTRON MICROSCOPY; ELECTROPHORESIS; ENZYME STRUCTURE; ENZYME SUBUNIT; FRAGMENTATION REACTION; GENE SEQUENCE; GENETIC CONSERVATION; GENOME; HYDROPHOBICITY; MAMMAL; MASS SPECTROMETRY; MITOCHONDRION; PREDICTION; PRIORITY JOURNAL; REVIEW; YARROWIA LIPOLYTICA; YEAST;

AMINO ACID SEQUENCE; BASE SEQUENCE; ELECTRON TRANSPORT COMPLEX I; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN SUBUNITS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; YARROWIA;

MAMMALIA; YARROWIA LIPOLYTICA;

EID: 3543015013     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.04.019     Document Type: Review

References (37)

1. Hofhaus G., Weiss H., Leonard K. Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J. Mol. Biol. 221:1991;1027-1043
2. 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
3. Grigorieff N. Three-dimensional structure of bovine NADH: ubiquinone oxidoreductase (Complex I) at 22 Å in ice. J. Mol. Biol. 277:1998;1033-1046
4. Djafarzadeh R., Kerscher S., Zwicker K., Radermacher M., Lindahl M., Schägger H., Brandt U. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta. 1459:2000;230-238
5. Robinson B.H. Human Complex I deficiency: clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect. Biochim. Biophys. Acta. 1364:1998;271-286
6. Schapira A.H. Human complex I defects in neurodegenerative diseases. Biochim. Biophys. Acta. 1364:1998;261-270
7. Smeitink J., Van den Heuvel L. Human mitochondrial complex I in health and disease. Am. J. Hum. Genet. 64:1999;1505-1510
8. Schon E.A. Mitochondrial genetics and disease. Trends Biochem. Sci. 25:2000;555-560
9. Yagi T., Yano T., Di Bernardo S., Matsuno-Yagi A. Procaryotic complex I (NDH-1), an overview. Biochim. Biophys. Acta. 1364:1998;125-133
10. Ohnishi T. Iron-sulfur clusters semiquinones in complex I. Biochim. Biophys. Acta. 1364:1998;186-206
11. Carroll J., Fearnley I.M., Shannon R.J., Hirst J., Walker J.E. Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell. Proteomics. 2:2003;117-126
12. Hirst J., Carroll J., Fearnley I.M., Shannon R.J., Walker J.E. The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim. Biophys. Acta. 1604:2003;135-150
13. Videira A., Duarte M. From NADH to ubiquinone in Neurospora crassa. Biochim. Biophys. Acta. 1555:2002;187-191
14. Kerscher S., Dröse S., Zwicker K., Zickermann V., Brandt U. Yarrowia lipolytica, a yeast genetic system to study mitochondrial complex I. Biochim. Biophys. Acta. 1555:2002;83-91
15. Kerscher S., Durstewitz G., Casaregola S., Gaillardin C., Brandt U. The complete mitochondrial genome of Yarrowia lipolytica. Compar. Funct. Genom. 2:2001;80-90
16. Kashani-Poor N., Kerscher S., Zickermann V., Brandt U. Efficient large scale purification of his-tagged proton translocating NADH: ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta. 1504:2001;363-370
17. Finel M., Skehel J.M., Albracht S.P.J., Fearnley I.M., Walker J.E. Resolution of NADH: ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry. 31:1992;11425-11434
18. Rais I., Karas M., Schägger H. Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics. 2004;. (in press)
19. Marchler-Bauer A., Anderson J.B., DeWeese-Scott C., Fedorova N.D., Geer L.Y., He S., Hurwitz D.I., Jackson J.D., Jacobs A.R., Lanczycki C.J., Liebert C.A., Liu C., Madej T., Marchler G.H., Mazumder R., Nikolskaya A.N., Panchenko A.R., Rao B.S., Shoemaker B.A., Simonyan V., Song J.S., Thiessen R.A., Vasudevan S., Wang Y., Yamashita R.A., Yin J.J., Bryant S.H. CDD: a curated Entrez database of conserved domain alignments. Nucleic Acids Res. 31:2003;383-387
20. Tusnady G.E., Simon I. Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol. 283:1998;489-506
21. Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:2001;567-580
22. Zickermann V., Bostina M., Hunte C., Ruiz T., Radermacher M., Brandt U. Functional implications from an unexpected position of the 49 kDa subunit of complex I. J. Biol. Chem. 278:2003;29072-29078
23. Yamaguchi M., Belogrudov G., Matsuno-Yagi A., Hatefi Y. The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH: ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 267:2000;329-336
24. Schulte U., Haupt V., Abelmann A., Fecke W., Brors B., Rasmussen T., Friedrich T., Weiss H. A reductase/isomerase subunit of mitochondrial NADH: ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex. J. Mol. Biol. 292:1999;569-580
25. Papa S. The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade. Biochim. Biophys. Acta. 1555:2002;147-153
26. Carroll J., Shannon R.J., Fearnley I.M., Walker J.E., Hirst J. Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I - identification of two new subunits. J. Biol. Chem. 277:2002;50311-50317
27. Fearnley I.M., Carroll J., Shannon R.J., Runswick M.J., Walker J.E., Hirst J. Grim-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH: ubiquinone oxidoreductase (complex I). J. Biol. Chem. 276:2001;38345-38348
28. Lufei C., Ma J., Huang G., Zhang T., Novotny-Diermayr V., Ong C.T., Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 22:2003;1325-1335
29. Angell J.E., Lindner D.J., Shapiro P.S., Hofmann E.R., Kalvakolanu D.V. Identification of GRIM-19, a Novel cell death-regulatory gene induced by the interferon-β and retinoic acid combination, using a genetic approach. J. Biol. Chem. 275:2000;33416-33426
30. Runswick M.J., Fearnley I.M., Skehel J.M., Walker J.E. Presence of an acyl carrier protein in NADH: ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 286:1991;121-124
31. Sackmann U., Zensen R., Roehlen D., Jahnke U., Weiss H. The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH: ubiquinone reductase (complex I). Eur. J. Biochem. 200:1991;463-469
32. Jordan S.W., Cronan J.E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272:1997;17903-17906
33. Schulte U. Biogenesis of respiratory complex I. J. Bioenerg. Biomembranes. 33:2001;205-212
34. Scheffler I.E., Yadava N. Molecular genetics of the mammalian NADH-ubiquinone oxidoreductase. J. Bioenerg. Biomembranes. 33:2001;243-250
35. 1 complex. J. Biol. Chem. 269:1994;12947-12953
36. Madeo F., Engelhardt S., Herker E., Lehmann N., Maldener C., Proksch A., Wissing S., Fröhlich K.-U. Apoptosis in yeast: a new model system with applications in cell biology and medicine. Curr. Genet. 41:2002;208-216
37. Mazzoni C., Mancini P., Verdone L., Madeo F., Serafini A., Herker E., Falcone C. A truncated form of KlLsm4p and the absence of factors involved in mRNA decapping trigger apoptosis in yeast. Mol. Biol. Cell. 14:2003;721-729