Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: Identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry

Protein Science

Volumn 6, Issue 11, 1997, Pages 2426-2435

  Gillet, Sylvie ^a   Hountondji, Codjo ^a   Schmitter, Jean Marie ^a   Blanquet, Sylvain ^a  

^a LABORATOIRE DE BIOCHIMIE   (France)

Author keywords

Isopeptide bond; MALDI MS; Methionyl adenylate; Methionyl tRNA synthetase; Methionylated lysyl residues; Post translational modification

Indexed keywords

ADENOSINE PHOSPHATE; AMINO ACID; LYSINE; METHIONINE; METHIONINE TRANSFER RNA LIGASE;

ARTICLE; COVALENT BOND; ENZYME ACTIVITY; ENZYME MODIFICATION; ESCHERICHIA COLI; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

ESCHERICHIA COLI;

EID: 0030711763     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061116     Document Type: Article

References (46)

1. Blanquet S, Fayat G, Waller JP, Iwatsubo M. 1972. The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction. Eur J Biochem 24:461-469.
2. Blanquet S, Fayat G., Waller JP. 1974. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli: Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes. Eur J Biochem 44:343-35.
3. Brunie S, Zelwer C, Risler JL. 1990. Crystallographic study at 2.5 Å resolution of the interaction of methionyl-tRNA synthetase of Escherichia coli with ATP. J Mol Biol 216:411-424.
4. Cusack S, Berthet-Colominas C, Härtlein M, Nassar N, Leherman R. 1990. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347:249-255.
5. Dardel F, Fayat G, Blanquet S. 1984. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene. J Bacteriol 160:1115-1122.
6. Eriani G, Delarue M, Poch O, Gangloff J, Moras D. 1990. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347:201-206.
7. Fourmy D, Mechulam Y, Brunie S, Blanquet S, Fayat G. 1991. Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase. FEBS Lett 292:259-263.
8. Fourmy D, Meinnel T, Mechulam Y, Blanquet S. 1993. Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase. J Mol Biol 231:1068-1077.
9. Gale A, Shi JP, Schimmel P. 1996. Evidence that specificity of microhelix charging by a class I tRNA synthetase occurs in the transition state of catalysis. Biochemistry 35:608-615.
10. Ghosh G, Pelka H, Schulman LD, Brunie S. 1991. Activation of methionine by Escherichia coli methionyl-tRNA synthetase. Biochemistry 30:9569-9575.
11. Guillon JM, Meinnel T, Mechulam Y, Lazennec C, Blanquet S, Fayat G. 1992. Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAfMet formyltransferase. J Mol Biol 224:359-367.
12. Hountondji C, Fayat G, Blanquet S. 1979. Complete inactivation and labeling of methionyl-tRNA synthetase by periodate-treated initiator tRNA in the presence of sodium cyanohydridoborate. Eur J Biochem 102:247-250.
13. fMet. Biochemistry 24:1175-1180.
14. Hountondji C, Lederer F, Dessen P, Blanquet S. 1986a. Escherichia coli tyrosyl-and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3′-end of tRNA. Biochemistry 25:16-21.
15. Hountondji C, Dessen P, Blanquet S. 1986b. Sequence similarities among the family of aminoacyl-tRNA synthetases. Biochimie 68:1071-1078.
16. Hountondji C, Schmitter JM, Fukui T, Tagaya M, Blanquet S. 1990a. Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl-and valyl-tRNA synthetases. Biochemistry 29:11266-11273.
17. Hountondji C, Schmitter JM, Beauvallet C, Blanquet S. 1990b. Mapping of the active site of Escherichia coli methionyl-tRNA synthetase: Identification of amino acid residues labeled by periodate-oxidized tRNAfMet molecules having modified lengths at the 3′ acceptor end. Biochemistry 29:8190-8198.
18. Hyafil F, Jacques Y, Fayat G, Fromant M, Dessen P, Blanquet S. 1976. Methionyl-tRNA synthetase from Escherichia coli: Active stoichiometry and stopped-flow analysis of methionyl adenylate formation. Biochemistry 15:3678-3685.
19. 3H-amino acids into proteins in a partially purified fraction of axoplasm: Evidence for transfer RNA-mediated. post-translational protein modification in squid giant axons. J Neurosci 3:2463-2473.
20. Jacques Y, Blanquet S. 1977. Interrelation between transfer RNA and amino-acid-activating sites of methionyl transfer RNA synthetase from Escherichia coli. Eur J Biochem 79:433-441.
21. Kalogerakos T, Hountondji C, Berne PF, Dutka S, Blanquet S. 1994. Modification of aminoacyl-tRNA synthetases with pyridoxal-5′-phosphate. Identification of the labeled amino acid residues. Biochimie 76:33-44.
22. Kern D, Lorber B, Boulanger Y, Giegé R. 1985. A peculiar property of aspartyltRNA synthetase from bakers' yeast: Chemical modification of the protein by enzymatically synthesized aminoacyl adenylate. Biochemistry 24:1321-1332.
23. Kim S, Landro J, Gale A, Schimmel P. 1993. C-terminal peptide appendix in a class I tRNA synthetase needed for acceptor-helix contacts and microhelix aminoacylation. Biochemistry 32:13026-13031.
24. Kleinkauf H, Von Döhren H. 1990. Nonribosomal biosynthesis ot peptide anti-biotics. Eur J Biochem 192:1-15.
25. Kovaleva GK, Moroz SG, Favorova OO, Kisselev LL. 1978. Tryptophanyl-tRNA synthetase: Evidence for an anhydrous bond involved in the tryptophanyl enzyme formation. FEBS Lett 95:81-84.
26. Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure. J Appl Crystallogr 24:946-950.
27. Landès C, Perona JJ, Brunie S, Rould MA, Zelwer C, Steitz TA, Risler JL. 1995. A structure-based multiple sequence alignment of class I aminoacyl-tRNA synthetases. Biochimie 77:194-203.
28. Landro J, Schimmel P. 1993. Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide binding fold. Proc Natl Acad Sci USA 90:2261-2265.
29. Lawrence F, Blanquet S, Poiret S, Robert-Gero M, Waller JP. 1973. The mechanism of action of methionyl-tRNA synthetase 3. Ion requirement and kinetic parameters of ATP-PPi and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes. Eur J Biochem 36:234-243.
30. Leibowit MJ, Soffer RL. 1971a. Enzymatic modification of proteins. VI. Site of acylation of bovine serum albumin in the leucine, phenylalanine-transfer reaction. J Biol Chem 240:4431-4438.
31. Leibowitz MJ, Soffer RL. 197Ib. Enzymatic modification of proteins. VII. Substrate specificity of leucyl, phenylalanyl-transfer ribonucleic acid-protein transferase. J Biol Chem 246:5207-5212.
32. Leon O, Schulman LH, 1987. tRNA recognition site of Escherichia coli methionyl-tRNA synthetase. Biochemistry 26:5416-5422.
33. Lorber B, Kern D, Giegé R, Ebel JP. 1982. Cuvalent attachment of aspartic acid to yeast aspartyl-tRNA synthetase induced by the enzyme. FEBS Lett 146:59-64.
34. Martinis S, Schimmel P. 1992. Enzymatic aminoacylation of sequence-specific RNA minihelices and hybride duplexes with methionine. Proc Natl Acad Sci USA 89:65-69.
35. Mechulam Y, Dardel F, Le Corre D, Blanquet S, Fayat G. 1991. Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase of Escherichia coli. J Mol Biol 217:465-475.
36. Met expressed from a synthetic gene in vivo. Nucleic Acid Res 16:8095-8096.
37. Meinnel T, Mechulam Y, Le Corre D, Panvert M, Blanquet S, Fayat G. 1991. Selection of suppressor methionyl-tRNA synthetases: Mapping of the tRNA anticodon binding site. Proc Natl Acad Sci USA 88:291-295.
38. Mejdoub H, Kern D, Giegé R, Ebel JP, Boulanger Y, Reinbolt J. 1987. Covalent asparlylation of aspartyl-tRNA synthetase from bakers' yeast by its cognate aspartyl adenylate: Identification of the labeled residues. Biochemistry 26:2054-2059.
39. Mellot P, Mechulam Y, Le Corre D, Blanquet S, Fayat G. 1989. Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition. J Mol Biol 208:429-443.
40. Nakajima H, Kitabatake S, Tsurutani R, Yamamoto K, Tomioka I, Imahori K. 1986. Dipeptide synthesis catalyzed by aminoacyl-tRNA synthetases from Bacillus stearothcrmophilus. Int J Pept Protein Res 28:179-185.
41. Pavela-Vrancic M, Van Liempt H, Pfeifer E, Freist W, Von Döhren H. 1994. Nucleotide binding by multienzyme peptide synthetases. Eur J Biochem 220:535-542.
42. Rapaport E, Yogeeswaran G, Zamecnik PC, Rémy P. 1985. Covalent Modification of phenylalanyl-tRNA synthetase with phenylalanine during the amino acid activation reaction catalyzed by the enzyme. J Biol Chem 260:9509-9512.
43. Soffer RL. 1971. Enzymatic modification of proteins. V. Protein acceptor specificity in the arginine-transfer reaction. J Biol Chem 246:1602-1606.
44. Softer RL. 1973. Peptide acceptors in the leucine, phenylalanine transfer reaction. J Biol Chem 248:8424-8428.
45. Valenzuela D, Schulman LD. 1986. Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase. Biochemistry 25:4555-4561.
46. Zanakis MF, Chakraborty G, Sturman JA, Ingoglia NA. 1984. Posttranslational protein modification by amino acid addition in intact and regenerating axons of the rat sciaic nerve. J Neurochem 43:1286-1294.