Characterization of Gtf1p, the connector subunit of yeast mitochondrial tRNA-dependent amidotransferase

Journal of Biological Chemistry

Volumn 286, Issue 38, 2011, Pages 32937-32947

  Barros, Mario H ^a   Rak, Malgorzata ^b   Paulela, Janaina A ^a   Tzagoloff, Alexander ^b  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP SYNTHASE; CATALYTIC SUBUNITS; CYTOCHROME OXIDASE; IN-VIVO; OVER-EXPRESSION; RESPIRATORY SUBSTRATES; TEMPERATURE-SENSITIVE; TRANSAMIDATION;

CATALYSIS; GENES; MITOCHONDRIA;

YEAST;

CYTOCHROME C OXIDASE; GLUTAMINE TRANSFER RNA; GLUTAMINE TRANSFER RNA LIGASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; CONTROLLED STUDY; ELECTROPHORESIS; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME SUBSTRATE; ENZYME SUBUNIT; ENZYME SYNTHESIS; FUNGAL GENE; GENE OVEREXPRESSION; HER2 GENE; MITOCHONDRION; NONHUMAN; PET112 GENE; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; YEAST CELL;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; AMINO ACYL-TRNA SYNTHETASES; ANTIMYCIN A; GENE EXPRESSION REGULATION, FUNGAL; GENES, MITOCHONDRIAL; MITOCHONDRIA; MUTATION; NADH DEHYDROGENASE; NITROGENOUS GROUP TRANSFERASES; PEPTIDES; PHENOTYPE; PROTEIN BIOSYNTHESIS; PROTEIN SUBUNITS; PROTEIN TRANSPORT; RNA, MESSENGER; RNA, TRANSFER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE;

BACTERIA (MICROORGANISMS); SACCHAROMYCES CEREVISIAE;

EID: 80053045925     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.265371     Document Type: Article

References (59)

1. Wilcox, M., and Nirenberg, M. (1968) Proc. Natl. Acad. Sci. U.S.A. 61, 229-236
2. Lapointe, J., Duplain, L., and Proulx, M. (1986) J. Bacteriol. 165, 88-93
3. Frechin, M., Senger, B., Brayé, M., Kern, D., Martin, R. P., and Becker, H. D. (2009) Genes Dev. 23, 1119-1130
4. Schön, A., Hottinger, H., and Söll, D. (1988) Biochimie 70, 391-394
5. Pujol, C., Bailly, M., Kern, D., Maréchal-Drouard, L., Becker, H., and Duchêne, A. M. (2008) Proc. Natl. Acad. Sc.i U.S.A. 105, 6481-6485
6. Nagao, A., Suzuki, T., Katoh, T., Sakaguchi, Y., and Suzuki, T. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 16209-16214
7. Curnow, A. W., Hong, K., Yuan, R., Kim, S., Martins, O., Winkler, W., Henkin, T. M., and Söll, D. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 11819-11826
8. Becker, H. D., and Kern, D. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 12832-12837
9. Wilcox, M. (1969) Eur. J. Biochem. 11, 405-412
10. Feng, L., Sheppard, K., Tumbula-Hansen, D., and Söll, D. (2005) J. Biol. Chem. 280, 8150-8155
11. Nakamura, A., Yao, M., Chimnaronk, S., Sakai, N., and Tanaka, I. (2006) Science 312, 1954-1958
12. Mulero, J. J., Rosenthal, J. K., and Fox, T. D. (1994) Curr. Genet. 25, 299-304
13. Kim, S. I., Stange-Thomann, N., Martins, O., Hong, K. W., Söll, D., and Fox, T. D. (1997) J. Bacteriol. 179, 5625-5627
14. Rinehart, J., Krett, B., Rubio, M. A., Alfonzo, J. D., and Söll, D. (2005) Genes Dev. 19, 583-592
15. Barros, M. H., Myers, A. M., Van Driesche, S., and Tzagoloff, A. (2006) J. Biol. Chem. 281, 3743-3751
16. Rak, M., Tetaud, E., Godard, F., Sagot, I., Salin, B., Duvezin-Caubet, S., Slonimski, P. P., Rytka, J., and di Rago, J. P. (2007) J. Biol. Chem. 282, 10853-10864
17. Barros, M. H., Nobrega, F. G., and Tzagoloff, A. (2002) J. Biol. Chem. 277, 9997-10002
18. Hell, K., Tzagoloff, A., Neupert, W., and Stuart, R. A. (2000) J. Biol. Chem. 275, 4571-4578
19. Tzagoloff, A., and Dieckmann, C. L., (1990) Microbiol. Rev. 54, 211-225
20. Myers, A. M., Pape, K. L., and Tzagoloff, A. (1985) EMBO J. 4, 2087-2092
21. Faye, G., Kujawa, C., and Fukuhara, H. (1974) J. Mol. Biol. 88, 185-203
22. Gietz, R. D., and Sugino, A. (1988) Gene 74, 527-534
23. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
24. Schiestl, R. H., and Gietz, R. D. (1989) Curr. Genet. 16, 339-346
25. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randal, R. J. (1951) J. Biol. Chem. 193, 265-275
26. Tzagoloff, A., Akai, A., and Needleman, R. B. (1975) J. Biol. Chem. 250, 8228-8235
27. Laemmli, U. K. (1970) Nature 227, 680-685
28. Broach, J. R., Strathern, J. N., and Hicks, J. B. (1979) Gene 8, 121-133
29. Ackerman, S. H., and Tzagoloff, A. (2005) Prog. Nucleic Acid Res. Mol. Biol. 80, 95-133
30. Tzagoloff, A. (1969) J. Biol. Chem. 244, 5020-5026
31. Barrientos, A., Korr, D., and Tzagoloff, A. (2002) EMBO J. 21, 43-52
32. Schneider, A., Behrens, M., Scherer, P., Pratje, E., Michaelis, G., and Schatz, G. (1991) EMBO J. 10, 247-254
33. Hell, K., Herrmann, J., Pratje, E., Neupert, W., and Stuart, R. A. (1997) FEBS Lett. 418, 367-370
34. Green-Willms, N. S., Butler, C. A., Dunstan, H. M., and Fox, T. D. (2001) J. Biol. Chem. 276, 6392-6397
35. Poutre, C. G., and Fox, T. D. (1987) Genetics 115, 637-647
36. Rak, M., and Tzagoloff, A. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 18509-18514
37. Paul, M. F., Barrientos, A., and Tzagoloff, A. (2000) J. Biol. Chem. 275, 29238-29243
38. Jan, P. S., Esser, K., Pratje, E., and Michaelis, G. (2000) Mol. Gen. Genet. 263, 483-491
39. Herrmann, J. M., Fölsch, H., Neupert, W., and Stuart, R. A. (1994) in Cell Biology: A Laboratory Handbook, Vol. 1 (Celis, D. E., ed) pp. 538-544, Academic Press, Inc., San Diego
40. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., and Yoshikawa, S. (1996) Science. 272, 1136-1144
41. Herrmann, J. M., Koll, H., Cook, R. A., Neupert, W., and Stuart, R. A. (1995) J. Biol. Chem. 270, 27079-27086
42. He, S., and Fox, T. D. (1999) Mol. Cell. Biol. 19, 6598-6607
43. Simon, M., and Faye, G. (1984) Mol. Gen. Genet. 196, 266-274
44. Nakagawa, K., Morishima, N., and Shibata, T. (1991) J. Biol. Chem. 266, 1977-1984
45. Pélissier, P., Camougrand, N., Velours, G., and Guérin, M. (1995) Curr. Genet. 27, 409-416
46. Dieckmann, C. L., and Staples, R. R. (1994) Int. Rev. Cytol. 152, 145-181
47. Law, R. H., Farrell, L. B., Nero, D., Devenish, R. J., and Nagley, P. (1988) FEBS Lett. 236, 501-505
48. Supekova, L., Supek, F., Greer, J. E., and Schultz, P. G. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 5047-5052
49. Steele, D. F., Butler, C. A., and Fox, T. D. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 5253-5257
50. Claros, M. G., and Vincens, P. (1996) Eur. J. Biochem. 241, 779-786
51. Glick, B. S., and Pon, L. A. (1995) Methods Enzymol. 260, 213-223
52. He, S., and Fox, T. D. (1997) Mol. Biol. Cell. 8, 1449-1460
53. Soto, I. C., Fontanesi, F., Valledor, M., Horn, D., Singh, R., and Barrientos, A. (2009) Biochim. Biophys. Acta 1793, 1776-1786
54. Terpstra, P., and Butow, R. A. (1979) J. Biol. Chem. 254, 12662-12669
55. Stanzel, M., Schön, A., and Sprinzl, M. (1994) Eur. J. Biochem. 15, 435-439
56. Nagao, A., Suzuki, T., and Suzuki, T. (2007) Nucleic Acids Symp. Ser. 41-42
57. Roy, H., Becker, H. D., Mazauric, M. H., and Kern, D. (2007) Nucleic Acids Res. 35, 3420-3430
58. Pelchat, M., Lacoste, L., Yang, F., and Lapointe, J. (1998) Can. J. Microbiol. 44, 378-381
59. Min, B., Kitabatake, M., Polycarpo, C., Pelaschier, J., Raczniak, G., Ruan, B., Kobayashi, H., Namgoong, S., and Söll, D. (2003) J. Bacteriol. 185, 3524-3526