The post-translational modifications of the nuclear encoded subunits of complex I from bovine heart mitochondria

Molecular and Cellular Proteomics

Volumn 4, Issue 5, 2005, Pages 693-699

  Carroll, Joe ^a   Fearnley, Ian M ^a   Skehel, J Mark ^b   Runswick, Michael J ^a   Shannon, Richard J ^a   Hirst, Judy ^a   Walker, John E ^a  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

^b GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; HISTIDINE; METHYL GROUP; MITOCHONDRIAL DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

ACETYLATION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CATTLE; CELL NUCLEUS; CELL ORGANELLE; CHEMICAL COMPOSITION; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME SUBUNIT; EXTRACELLULAR MATRIX; EXTRACELLULAR SPACE; HEART MITOCHONDRION; INTRACELLULAR TRANSPORT; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; METHYLATION; MOLECULAR WEIGHT; MYRISTYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROCESSING;

ANIMALS; CATTLE; CELL NUCLEUS; ELECTRON TRANSPORT COMPLEX I; MITOCHONDRIA, HEART; PROTEIN PROCESSING, POST-TRANSLATIONAL; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

BOVINAE; MAMMALIA;

EID: 20844449723     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500014-MCP200     Document Type: Article

References (30)

1. Walker, J. E. (1992) The NADH-ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25, 253-324
2. Grigorieff, N. (1998) Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277, 1033-1046
3. Wikström, M. (1984) Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett. 169, 300-304
4. Walker, J. E., Arizmendi, J. M., Dupuis, A., Fearnley, I. M., Finel, M., Medd, S, M., Pilkington, S. J., Runswick, M. J., and Skehel, J. M. (1992) Sequences of twenty subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria: application of a novel strategy for sequencing proteins using the polymerase chain reaction. J. Mol. Biol. 226, 1051-1072
5. Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., and Hirst, J. (2001) GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 276, 38345-38348
6. Carroll, J., Shannon, R. J., Fearnley, I. M., Walker, J. E., and Hirst, J. (2002) Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits. J. Biol. Chem. 277, 50311-50317
7. Carroll, J., Fearnley, I. M., Shannon, R. J., Hirst, J., and Walker, J. E. (2003) Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell. Proteomics 2, 117-126
8. Anderson, S., de Bruijn, M. H., Coulson, A. R., Eperon, I. C., Sanger, F., and Young, I. G. (1982) Complete sequence of bovine mitochondrial DNA. J. Mol. Biol. 156, 683-717
9. Chomyn, A., Mariottini, P., Cleeter, M. W. J., Ragan, C. I., Matsuno-Yagi, A., Hatefi, Y., Doolittle, R. F., and Attardi, G. (1985) Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory chain NADH dehydrogenase. Nature 314, 592-597
10. Chomyn, A., Cleeter, M. W. J., Ragan, C. I., Riley, M., Doolittle, R. F., and Attardi, G. (1986) Last unidentified reading frame of human mtDNA codes for an NADH dehydrogenase subunit. Science 234, 614-618
11. Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., and Walker, J. E. (2003) The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim. Biophys. Acta 1604, 135-150
12. Fearnley, I. M., Skehel, J. M., and Walker, J. E. (1994) Electrospray mass spectrometric analysis of subunits of NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Biochem. Sac. Trans. 22, 551-555
13. Skehel, J. M., Fearnley, I. M., and Walker, J. E. (1998) NADH:ubiquinone oxidoreductase from bovine heart mitochondria: sequence of a novel 17.2 kDa subunit. FEBS Lett. 438, 301-305
14. Smith, A. L. (1967) Preparation, properties and conditions for assay of mitochondria: slaughterhouse material, small scale. Methods Enzymol. 10, 81-86
15. Walker, J. E., Skehel, J. M., and Buchanan, S. K. (1995) Structural analysis of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Methods Enzymol. 260, 14-34
16. Sazanov, L. A., Peak-Chew, S. Y., Fearnley, I. M., and Walker, J. E. (2000) Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry 39, 7229-7235
17. Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469
18. van Montfort, B. A., Canas, B., Duurkens, R., Godovac-Zimmermann, J., and Robillard, G. T. (2002) Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time of flight mass spectrometry. J. Mass Spectrom. 37, 322-330
19. Arizmendi, J. M., Skehel, J. M., Runswick, M. J., Fearnley, I. M., and Walker, J. E. (1992) Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Completion of the primary structure of the complex? FEBS Lett. 313, 80-84
20. Tsunasawa, S., and Sakiyama, F. (1984) Amino terminal acetylation of proteins: an overview. Methods Enzymol. 106, 165-170
21. Redman, K. L., and Rubenstein, P. A. (1984) Actin amino terminal acetylation and processing in a rabbit reticulocyte lysate. Methods Enzymol. 106, 179-192
22. Towler, D. A., Adams, S. P., Eubanks, S. R., Towery, D. S., Jackson-Machelski, E., Glaser, L., and Gordon J. I. (1988) Myristoyl CoA:protein myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities. J. Biol. Chem. 263, 1784-1790
23. Yadav, N., Lee, J., Kim, J., Shen, J., Hu, M. C.-T., Aldaz, C. M., and Bedford, M. T. (2003) Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 100, 6464-6468
24. Kalhor, H. R. Niewmierzycka, A., Faull, K. F., Yao, X., Grade, S., Clarke, S., and Rubenstein P. A. (1999) A highly conserved 3-methylhistidine modification is absent in yeast actin. Arch. Biochem. Biophys. 370, 105-111
25. Huszar, G. (1984) Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences. Methods Enzymol. 106, 287-291
26. 73 of yeast actin. J. Biol. Chem. 274, 37443-37449
27. Brodsky, I. G., Suzara, D., Hornberger, T. A., Goldspink, P., Yarasheski, K. E., Smith, S., Kukowski, J., Esser, K., Bedno, S. (2004) Isoenergetic dietary protein restriction decreases myosin heavy chain IIx fraction and myosin heavy chain production in humans. J. Nutr. 134, 328-334
28. Grabarse, W., Mahlert, F., Shima, S., Thauer, R. K., and Ermler, U. (2000) Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation. J. Mol. Biol. 303, 329-344
29. Aletta, J. M., Cimato, T. R., and Ettinger, M. J. (1998) Protein methylation: a signal event in post-translational modification. Trends Biochem. Sci. 23, 89-91
30. Runswick, M. J., Fearnley, I. M., Skehel, J. M., and Walker, J. E. (1991) Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 286, 121-124