Methionine Analogue Probes Functionally Important Residues in Active Site of Methionyl-tRNA Synthetase

Journal of Biochemistry and Molecular Biology

Volumn 32, Issue 6, 1999, Pages 547-553

  Jo, Yeong Joon ^a   Lee, Sang Won ^a   Jo, Myung Kyun ^a   Lee, Jee Woo ^b   Kang, Mee Kyoung ^b   Yoon, Jeong Hyeok ^c   Kim, Sunghoon ^a  

^a Natl Creative Res Initiatives C   (South Korea)

^b Seoul National University   (South Korea)

^c Sungkyunkwan University   (South Korea)

Author keywords

Active site; Functional residues; L Methionine hydroxamate; Methionyl tRNA synthetase

Indexed keywords

EID: 0000612893     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (41)

1. Brunie, S., Zelwer, C. and Risler, J. L. (1990) Crystallographic study at 2.5 Å resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP. J. Mol. Biol. 216, 411-424.
2. Burbaum, J. J., Starzyk, R. M. and Schimmel, P. (1990) Understanding structure relationships in proteins of unsolved three-dimensional structure. Proteins Struct. Funct. Genet. 7, 99-111.
3. Cassio, D. and Waller, J.-P. (1971) Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme. Eur. J. Biochem. 20, 283-300.
4. Cusack, S., Berthet-Colominas, C., Härtlein, M., Nassar, N. and Leberman, R. (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.4 Å. Nature 347, 249-255.
5. Eriani, G., Delarue, M., Poch, O., Gangloff, J. and Moras, D. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-206.
6. Fasiolo, F., Bonnet, J. and Lacroute, F. (1981) Cloning of the yeast methionyl-tRNA synthetase gene. J. Biol. Chem. 56, 2324-2328.
7. Fourmy, D., Mechulam, Y., Brunie, S., Blanquet, S. and Fayat, G. (1991) Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase. FEBS Lett. 292, 259-263.
8. Ghosh, G., Pelka, H. and Schulman, L. H. (1990) Identification of the tRNA anticodon recognition site of Escherichia coli methionyl-tRNA synthetase. Biochemistry 29, 2220-2225.
9. Ghosh, G., Pelka, H., Schulman, L. H. and Brunie, S. (1991) Activation of methionine by Escherichia coli methionyl-tRNA synthetase. Biochemistry 30, 9569-9575.
10. Gillet, S., Hountondji, C., Schmitter, J. M. and Blanquet, S. (1997) Covalent methionylation of Escherichia coli methionyl-tRNA synthetase: Identification of the labeled amino acid residues by matrix-assisted laser deposition-ionization mass spectrometry. Protein Sci. 6, 2426-2435.
11. Heacock, D., Forsyth, C. J., Shiba, K. and Musier-Forsyth, K. (1996) Synthesis and aminoacyl-tRNA synthetase inhibitory activity of prolyl adenylate analogs. Bioorganic Chemistry 24, 273-289.
12. Hipps, D., Shiba, K., Henderson, B. and Schimmel, P. (1995) Operational RNA code for amino acids: species-specific aminoacylation of minihelices switched by a single nucleotide. Proc. Natl. Acad. Sci. USA 92, 5550-5552.
13. Hou, Y. M. and Schimmel, P. (1988) A simple structural feature is a major determinant of the identity of a transfer RNA. Nature 333, 140-145.
14. Hountondji, C., Dessen, P. and Blanquet, S. (1986) Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3′-end of tRNA. Biochimie 68, 1071-1078.
15. Hountondji, C., Schmitter, J. M., Beavallet, C. and Blanquet, S. (1990) Mapping of the active site of Escherichia coli methionyl-tRNA synthetase: identification of amino acid residues labeled by periodate-oxidized tRNA(fMet) molecules having modified lengths at the 3′-acceptor end. Biochemistry 29, 8190-8198.
16. Karlin, S. and Altschul, S. F. (1990) Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Natl. Acad. Sci. USA 87, 2264-2268.
17. Kim, H. Y., Ghosh, G., Schulman, L. H., Brunie, S. and Jakubowski, H. (1993) The relationship between synthetic and editing functions of the active site of an aminoacyl-transfer RNA synthetase. Proc. Natl. Acad. Sci. USA 90, 11553-11557.
18. Kim, S. (1995) Quantitative analysis of protein-RNA interaction in a class I tRNA synthetase by saturation mutagenesis. J. Biochem. Mol. Biol. (formerly Korean Biochem. J.) 28, 363-367.
19. Kim, S. and Schimmel, P. (1992) Functional independence of microhelix aminoacylation from anticodon binding in a class I tRNA synthetase. J. Biol. Chem. 267, 15563-15567.
20. Kim, S. J. and Kim, S. (1997) Temperature sensitivity of a class I tRNA synthetase induced by artificial breakage of polypeptide chain. Mol. Cells 7, 389-393.
21. Kim, S., Jo, Y. J., Lee, S. H., Motegi, H., Shiba, K., Sassanfar, M. and Martinis, S. A. (1998) Biochemical and phylogenetic analyses of methionyl-tRNA synthetase isolated from a pathogenic microorganism, Mycobacterium tuberculosis. FEBS Lett. 427, 259-262.
22. Lage, H. and Dietel, M. (1996) Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene 178, 187-189.
23. Lamour, V., Quevillon, S., Diriong, S., N'Guyen, V. C., Lipinski, M. and Mirande, M. (1994) Evolution of the Glx-tRNA synthetase family: The glutaminyl enzyme as a case of horizontal gene transfer. Proc. Natl. Acad. Sci. USA 91, 8670-8674.
24. Lee, J. W., Kang, M. Y., Chun, M. W., Jo, Y. J., Kwak, J. H. and Kim, S. (1998a) Methionine analogues as inhibitors of methionyl-tRNA synthetase. Bioorg. Med. Chem. Lett. 8, 3511-3514.
25. Lee, S. W., Jo, Y. J. and Kim, S. (1998b) Cloning and characterization of mitochondrial methionyl-tRNA synthetase from a pathogenic fungi, Candida albicans. Gene 215, 311-318.
26. Ludmerer, S. W. and Schimmel, P. (1987) Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetase. J. Biol. Chem. 262, 10801-10806.
27. McClain, W. H. and Foss, K. (1988) Changing the acceptor identity of a transfer RNA by altering nucleotides in a "Variable Pocket". Science 241, 1804-1807.
28. Mellot, P., Mechulam, Y., Le Corre, D., Blanquet, S. and Fayat, G. (1989) Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition. J. Mol. Biol. 208, 429-443.
29. Nureki, O., Vassylyev, D. G., Katayanagi, K., Shimizu, T., Sekine, S., Kigawa, T., Miyazawa, T., Yokoyama, S. and Morikawa, K. (1995) Architectures of class-defining and specific domains of glutamyl-tRNA synthetase. Science 267, 1958-1965.
30. Perona, J. J., Rould, M. A., Steitz, T. A., Risler, J. L., Zelwer, C. and Brunie, S. (1991) Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggests a common overall orientation of tRNA binding. Proc. Natl. Acad. Sci. USA 88, 2903-2907.
31. Quinn, C. L., Tao, N. and Schimmel, P. (1995) Species-specific microhelix aminoacylation by a eukaryotic pathogen tRNA synthetase dependent on a single base pair. Biochemistry 34, 12489-12495.
32. Rho, S. B., Kim, M. J., Lee, J. S., Seol, W., Motegi, H., Kim, S. and Shiba, K. (1999) Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex. Proc. Natl. Acad. Sci. USA 96, 4488-4493.
33. Gln and ATP at 2.8 Å resolution. Science 246, 1135-1142.
34. Asp. Science 252, 1682-1689.
35. Schmitt, E., Panvert, M., Mechulam, Y. and Blanquet, S. (1997) General structure/function properties of microbial methionyl-tRNA synthetase. Eur. J. Biochem. 246, 539-547.
36. Shiba, K., Motegi, H. and Schimmel, P. (1997) Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains. Trends Biochem. Sci. 22, 453-457.
37. Starzyk, R. M. and Schimmel, P. (1989) Construction of interadomain chimeras of aminoacyl-tRNA synthetase. J. Biomol. Struct. Dyn. 7, 225-234.
38. Walter, P., Weygand-Durasevic, I., Sanni, A., Ebel, J.-P. and Fasiolo, F. (1989) Deletion analysis in the amino-terminal extension of methionyl-tRNA synthetase from Saccharomyces cerevisiae shows that a small region is important for the activity and stability of the enzyme. J. Biol. Chem. 264, 17126-17130.
39. Walter, R. D. and Kuhlow, F. (1985) Parasite-specific interaction of N-[4-(4′ nitroanilino)-phenyl]-S-(β-carboxylethyl)-dithiocarbamic acid-ester with arginyl-tRNA-synthetase from Dirofilaria immitis. Trop. Med. Parasitol. 36, 230-232.
40. Webster, T. A., Tsai, H., Kula, M., Mackie, G. A. and Schimmel, P. (1984) Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science 226, 1315-1317.
41. Yanagisawa, T., Lee, J. T., Wu, H. C. and Kawakami, M. (1994) Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli -proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase. J. Biol. Chem. 269, 24304-24309.