Glycyl-tRNA synthetase

Biological Chemistry Hoppe-Seyler

Volumn 377, Issue 6, 1996, Pages 343-356

  Freist, Wolfgang ^a   Logan, Derek T ^a   Gauss, Dieter H ^a  

^a MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

Author keywords

Glycyl tRNA synthetase

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE;

AMINO ACID METABOLISM; AMINOACYLATION; CELL FUNCTION; CRYSTAL STRUCTURE; INTERSTITIAL LUNG DISEASE; POLYMYOSITIS; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW;

ANIMALS; GLYCINE-TRNA LIGASE; HUMANS; PROTEIN STRUCTURE, SECONDARY;

EID: 0029794084     PISSN: 01773593     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (126)

1. Adams, M.D. et al. (1995). Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. Nature 377 Supplement, p.3-174(p.101).
2. Akhverdyan, V.Z., Kisselev, L.L, Knorre, D.G., Lavrik, O.I., and Nevinsky, G.A. (1977). Affinity labeling of tryptophanyl-transfer RNA synthetase, J. Mol. Biol. 113,475 - 501.
3. Anderson, R.P., and Roth, J.R. (1977). Tandem genetic duplications in phage and bacteria. Ann. Rev. Microbiol. 31,473 - 505.
4. Arbeeny, C.M., Briden, K.L., and Stirewalt, W.S. (1979). The activity and sedimentation properties of the aminoacyl-tRNA synthetases of rat skeletal muscle. Biochim. Biophys. Acta 564, 191-201.
5. Arnez, J.G., Harris, D.C., Mitschier, A., Rees, B., Francklyn, C.S., and Moras, D. (1995). Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBOJ. 74,4143-4155.
6. Bachmann, B.J., and Low, K.B. (1980). Linkage map of Escherichia coli K-12, edition 6. Microbiol. Rev. 44,1 - 56.
7. Beljanski, M. (1960). Synthesis of peptides by an enzyme system in the presence of nucleoside triphosphates. Compt. Rend. 250,624-625.
8. Berg, B.H. (1977). The early influence of 17-beta-estradiol on 17 aminoacyl-tRNA synthetases of mouse uterus and liver. Phosphorylation as a regulation mechanism. Biochim. Biophys. Acta479,152-171.
9. Berg, B.H. (1978). The role of cyclic 3', 5'-AMP in the regulation of aminoacyl-tRNA synthetase activities in mouse uterus and liver following 17-beta-estradiol treament: activation of a phosphoaminoacyl-tRNA synthetase phosphatase by phosphorylation with cyclic 3', 5'-AMP dependent protein kinase. Biochim. Biophys. Acta 52 7,274 - 287.
10. Berg, B.H. (1990). Chromatofocusing of aminoacyl-tRNA synthetases, extracted from NMRI mouse liver. Biochim. Biophys. Acta 7038,391-394.
11. Black, S., and Hazel, B. (1969). The activity of a glycyl transfer ribonucleic acid synthetase in the presence of inorganic sulfide. J. Biol. Chem. 244,1656 -1658.
12. Blanquet, S., Dessen, P., and Iwatsubo, M. (1976). Anticooperative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from Escherichia coli J. Mol. Biol. 703,765-784.
13. Bock, A., and Neidhardt, F.C. (1966). Location of the structural gene for glycyl ribonucleic acid synthetase by means of a strain of Escherichia coli possessing an unusual enzyme. Z. Vererbungslehre 98,187 -192. (CA 66:73525).
14. Boyko, J., and Fraser, M.J. (1964). Properties of rat liver glycyltRNA synthetase. Can. J. Biochem. 42,1677 -1695.
15. Brach, H., Cornillon, R., Lespinasse, J.N., and Vasilescu, D. (1976). Conformational analysis of aminoacyladenylates II: EHT study of glycyladenylate. J. Theoret. Biol. 57,407 - 418.
16. Bublitz, C. (1966). The properties of a glycyl-soluble-RNA synthetase from chick embryo. Biochim. Biophys. Acta 113, 158 166.
17. Burbaum, J.J., and Schimmel, P. (1991). Structural relationships and the classification of aminoacyl-tRNA synthetases. J. Biol. Chem. 266,16965-16968.
18. Capage, M., and Hill, C.W. (1979). Preferential unequal recombination in the glyS region of the Escherichia coli chromosome. J. Mol. Biol. 727,73-88.
19. Carbon, J., and Fleck, E.W. (1974). Genetic alteration of structure and function in glycine transfer RNA of Escherichia coli: mechanism of suppression of the tryptophan synthetase A78 mutation. J. Mot. Biol. 85,371 - 391.
20. Carter, C.W. (1993). Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Ann. Rev. Biochem. 62,715-748.
21. Cavarelli, J., Eriani, G., Rees, B., Ruff, M., Boeglin, M., Mitschler, A., Martin, F., Gangloff, J., Thierry, J.-C., and Moras, D. (1994). The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J., 73,327-337.
22. Cormier, M.J., and Novelli, G.D. (1958). The carboxyl activation of glycine in extracts of Photobacterium fischen. Biochim. Biophys. Acta 30,135-144.
23. Cramer, F., and Freist, W. (1993). Aminoacyl-tRNA synthetases: the division into two classes predicted by the chemistry of substrates and enzymes. Angew. Chem. Int. Ed. Engl. 32, 190 200.
24. Cusack, S. (1993). Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update. Biochimie 75,1077 -1081.
25. Cusack, S. (1995). Eleven down and nine to go. Nature Struct. Biol. 2,824-831.
26. Cusack, S., Härtlein, M., and Leberman, R. (1991). Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 79,3489 - 3498.
27. Dang, C.V., and Dang, C.V. (1986). Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic. Biochem. J. 239,249 - 255.
28. Delarue, M., and Moras, D. (1993). The aminoacyl-tRNA synthetase family: modules at work. BioEssays 75,675 - 687.
29. Del Monte, U., and Cini, G. (1970). Activity and kinetic behavior of some aminoacyl-tRNA synthetases of Yoshida hepatoma AH 130. Sperimentale 720,237 - 253. (CA 78:82722).
30. Dignam, S.S., and Dignam, J.D. (1984). Glycyl- and alanyl-tRNA synthetases from Bombyx mon: purification and properties. J. Biol. Chem. 259,4043 - 4048.
31. Dignam, S.S., and Dignam, J.D. (1988). Control of the levels of alanyl-, glycyl-, and seryl-tRNA synthetases in the silkgland of Bombyx mon. Dev. Biol. 729,350-357.
32. Ehrenfeld, G.M., Francis, TA, and Hecht, S.M. (1983). Loss of positional specificity in the aminoacylation of Escherichia coli tRNAGly. J. Biol. Chem. 258,11745 -11750.
33. 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.
34. Eriani, G., Cavarelli, J., Martin, F., Dirheimer, G., Moras, D., and Gangloff, J. (1993). Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline. Proc. Natl. Acad. Sei. USA 90,10816 -10820.
35. Favorova, O., and Kisselev, L. (1970). Glycyl-tRNA synthetase from rat liver: the role of tRNA in formation of glycylhydroxamates.FEBS-Lett.6,65-68.
36. Favorova, O.O., Spasukokotskaya, T.N., and Kisselev, L.L. (1968). Two forms of glycyl-tRNA synthetase in the rat liver. Mol. Biol. (Moscow) 2,69 - 78.
37. Feldmann, H., Mannhaupt, G., Schwarzlose, C., and Vetter, J. (1994). A probable gene of GlyRS from Saccharomyces cerevisiae. Submitted to EMBL Protein Sequence Data Base, PIR2: S44700, August 1994.
38. Fleischmann, R.D. étal. (1995). Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269,496-512.
39. Folk, W.R., and Berg, P. (1970a). Isolation and partial characterization of Escherichia coli mutants with altered glycyl transfer ribonucleic acid synthetases. J. Bacteriol. 702,193 - 203.
40. Folk, W.R., and Berg, P. (1970b). Characterization of altered forms of glycyl transfer ribonucleic acid synthetase and the effects of such alterations on aminoacyl transfer ribonucleic acid synthesis in vivo. J. Bacteriol. J02,204-212.
41. Folk, W.R., and Berg, P. (1971). Duplication of the structural gene for glycyl-transfer RNA synthetase in Escherichia coli. J. Mol. Biol. 58,595-610.
42. Francis, T.A., and Nagel, G.M. (1976). Glycyl-tRNA synthetase: evidence for two enzyme forms and sigmoidal saturation kinetics. Biochem. Biophys. Res. Commun. 70,862-868.
43. Francklyn, C., Shi, J.P., and Schimmel, P. (1992). Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices. Science 255,1121 -1125.
44. Fraser, C.M., et al. (1995). The minimal gene complement of Mycoplasma genitalium. Science 270,397 - 403.
45. Fraser, M.J. (1962). A sensitive method for measurement of amino acyl ribonucleic acid (RNA) synthetase activities. Can. J. Biochem. Physiol. 40,653 - 666.
46. Fraser, M.J. (1963). Glycyl-tRNA synthetase of rat liver: partial purification and effects of some metal ions on its activity. Can. J. Biochem. Physiol. 41,1123 -1133.
47. Freist, W., and Gauss, D.H. (1995). Threonyl-tRNA synthetase. Biol. Chem. Hoppe-Seyler376,213-224.
48. Freist, W., Sternbach, H., and Cramer, F. (1981). Survey on substrate specificity with regard to ATP analogs of aminoacyltRNA synthetases from £coli and from baker's yeast: correlation to synthetase families. Hoppe-Seyler's Z. Physiol. Chem. 362,1247-1254.
49. Ge, Q., Trieu, E.P., and Targoff, I.N. (1994). Primary structure and functional expression of human glycyl-tRNA synthetase, an autoantigen in myositis. J. Biol. Chem. 269,28790 - 28797.
50. Gibson, B.W., and Biemann, K. (1984). Strategy for the mass spectrometric verification and correction of the primary structures of proteins deduced from their DNA sequences. Proc. Natl. Acad. Sei. USA 81,1956 -1960.
51. Giegé, R., Puglisi, J.D., and Florentz, C. (1993). tRNA structure and aminoacylation efficiency. Progr. Nucl. Acid Res. Mol. Biol. 45,129-206.
52. Grosjean, H., Charlier, J., Darte, C., Dirheimer, G., Giegé, R., de
53. Henau, S., Keith, G., Parfait, R., and Takada, C. (1976). Purification, characterization and mechanism of action of several aminoacyl-tRNA synthetases from Bacillus stearothermophilus. In: Enzymes and Proteins from Thermophilic Microorganisms. Structure and Function. Experientia Suppl., Vol. 26, H. Zuber ed. (Basel, Switzerland: Birkhäuser), pp. 347 362.
54. 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. Sei. USA 92,5550 - 5552.
55. Hirakata, M., Mimori, T., Akizuki, M., Craft, J., Hardin, J.A., and Homma, M. (1992). Autoantibodies to small nuclear and cytöplasmic ribonucleoproteins in Japanese patients with inflammatory muscle disease. Arthritis Rheum. 35,449 - 456.
56. Hirakata, M., Suwa, A., Takeda, Y, Matsuoka, Y., Irimajiri, S., Targoff, I.N., Hardin, U.A., and Craft, J. (1996). Autoantibodies to glycyl-transfer RNA-synthetase in myositis - association with dermatomyositis and immunological heterogeneity. Arthritis Rheum. 39,146 -151.
57. Jakes, R., and Fersht, A.R. (1975). Tyrosyl-tRNA synthetase from Escherichia coli: Stoichiometry of ligand binding and half of the sites reactivity in aminoacylation. Biochemistry 14, 3344 3356.
58. Kawakami, M., and Nishio, K. (1985). Subunit structure and tRNA binding properties of Bombyx mon glycyl-tRNA synthetase. J. Biochem. 98,177-186.
59. Keng, T., and Schimmel, P. (1983). Synthesis of two polypeptide subunits of an aminoacyl-tRNA synthetase as a single polypeptide chain. J. Biomolec. Structure Dynamics 1,225-229.
60. Keng.T., Webster, T.A., Sauer, R.T., and Schimmel, P. (1982). Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding regions in the same reading frame. J. Biol. Chem. 257,12503-12508.
61. Kern, D., Giegé, R., and Ebel, J.P. (1981). Glycyl-tRNA synthetase from baker's yeast: interconversion between active and inactive forms of the enzyme. Biochemistry 20,122 -131.
62. Kern, D., and Lapointe, J. (1979). The twenty aminoacyl-tRNA synthetases from Escherichia coli: general separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities. Biochimie 67,1257 -1272.
63. Kiselev, N.A., Stelmashchuk, V.Y, Surgucheva, I.G., and Surguchev, A.P. (1976). Electron microscopy of glycyl-tRNA synthetase from Bacillus brevis. Dokl. Akad. Nauk SSSR 229, 217-219. (CA 85:105988).
64. Kisseiev, L.L., and Favorova, O.O. (1974). Aminoacyl-tRNA synthetases: some recent results and achievements. Adv. Enzymol. Relat. Areas Mol. Biol. 40,141 - 238.
65. Kisseiev, L.L., and Wolfson, A.D. (1994). Aminoacyl-tRNA synthetases from higher eukaryotes. Prog. Nucl. Acid Res. Mol. Biol. 48,83-142.
66. Kraulis, P.J. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24,946-950.
67. Kurosawa, S., Komano, T., and Onodera, K. (1972). Glycine activating enzyme in the posterior silkgland of silkworm. Agr. Biol. Chem. 36,779 - 784. (CA 77:71800).
68. Kurosawa, S., and Onodera, K. (1972). Correlation between two glycine tRNAs and corresponding glycyl tRNA synthetases. Agr. Biol. Chem. 36,1051 -1053. (CA 77:84876).
69. Lazdunski, M. (1972). Flip-flop mechanisms and half-site enzymes. Curr. Top. Cell. Regul. 6,267 - 310.
70. Lazdunski, M., Petitclerc, C., Chappelet, D., and Lazdunski, C. (1971). Flip-flop mechanisms in enzymology: a model: the alkaline phosphatase of Escherichia coli. Eur. J. Biochem. 20, 124-139.
71. Led, J. J., and Andersen, A.J. (1981 ). The use of paramagnetic 13C NMR relaxation to study the mechanisms of aminoacid activation catalyzed by a cognate tRNA synthetase. FEBS Lett. 724, 293-298.
72. Led, J.J., Switon, W.K., and Jensen, K.F. (1983). Phosphorolytic activity of Escherichia coli glycyl-tRNA synthetase towards its cognate aminoacyl adenylate detected by 31P-NMR spectroscopy and thinlayer chromatography. Eur. J. Biochem. 736, 469-479.
73. Loftfield, R.B. (1972). The mechanism of aminoacylation of transfer RNA. Prog. Nucleic Acid Res. Mol. Biol. 72,87 -128.
74. Logan, D.T., Cura, V., Touzel, J.-P., Kern, D., and Moras, D. (1994). Crystallisation of the glycyl-transfer RNA synthetase from Thermus thermophHus and initial crystallographic data. J. Mol. Biol.247,732-735.
75. Logan, D.T., Mazauric, M.-H., Kern, D., and Moras, D. (1995). Crystal structure of glycyl-tRNA synthetase from Thermus thermophHus. EMBO J. 14,4156-4167.
76. Malygin, E.G., and Degtyarev, S.Kh. (1983). Flip-flop mechanism of enhancement of the specificity of aminoacyl-tRNA synthetases. Mol. Biol. (Moscow) 7 7,118 -128.
77. Malygin, E.G., Zinoviev, V.V., Fasiolo, F., Kisselev, L.L, Kochkina, L.L., and Achverdyan, V.Z. (1976). Interaction of aminoacyltRNA synthetases and tRNA: positive and negative cooperativity of their active centres. Molec. Biol. Reports 2,445 - 454.
78. Martinis, S.A., and Schimmel, P. (1995). Small RNAoligonucleotide substrates for specific aminoacylation. In: tRNA: Structure, Biosynthesis and Function. D. Soil and U.L. RajBhandary, eds. (Washington D.C., USA: ASM Press), pp. 349-370.
79. McClain, W.H., Foss, K., Jenkins, R.A., and Schneider, J. (1991). Rapid determination of nucleotides that define tRNAGly acceptor identity. Proc. Natl. Acad. Sei. USA 88,6147-6151.
80. McDonald, T., Breite, L, Pangburn, K.L.W., Horn, S., Manser, J., and Nagel, G.M. (1980). Overproduction, purification, and subunit structure of Escherichia coli glycyl transfer ribonucleic acid synthetase. Biochemistry 79,1402 -1409.
81. Moras, D. (1993). Structural aspects and evolutionary implications of the recognition between tRNAs and aminoacyl-tRNA synthetases. Biochimie 75,651 -657.
82. Muench, K.H., and Berg, P. (1966). Preparation of aminoacyl ribonucleic acid synthetases from Escherichia coli. In: Procedures in Nucleic Acid Research. G.L. Cantoni and D.R. Davies, eds. (New York and London: Harper & Row), pp. 375 381.
83. Nada, S., Chang, P.K., and Dignam, J.D. (1993). Primary structure of the gene for glycyl-tRNA synthetase from Bombyx mon. J. Biol. Chem. 268, 7660 - 7667; (1995). Correction. J. Biol. Chem. 270,12948.
84. Nagel, G.M., Cumberledge, S., Johnson, M.S., Petrella, E., and Weber, B.H. (1984). The beta subunit of E.co//glycyI-tRNA synthetase plays a major role in tRNA recognition. Nucl. Acids Res. 72,4377-4384.
85. Nagel, G.M., Johnson, M.S., Rynd, J., Petrella, E., and Weber, B.H. (1988). Glycyl-tRNA synthetase of Escherichia coli: Immunological homology with phenylalanyl-tRNA synthetase. Arch. Biochem. Biophys. 262,409 - 415.
86. Neidhardt, F.C., Bloch, P.L, Pedersen, S., and Reeh, S. (1977). Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J. Bacteriol. 729,378-387.
87. Nichols, R.C., Pai, S.I., Ge, Q., Targoff, I.N., Plotz, P.H., and Liu, P. (1985). Localization of two human autoantigen genes by PCR screening and in situ hybridization: glycyl-tRNA synthetase locates to 7p15 and alanyl-tRNA synthetase to 16q22. Genomics 30,131-132.
88. Niyomporn, B., Dahl, J.L., and Strominger, J.L. (1968).
89. Biosynthesis of the peptidoglycan of bacterial cell walls: IX. purification and properties of glycyl transfer ribonucleic acid synthetase from Staphylococcus aureus. J. Biol. Chem. 243,773 778.
90. Niyomporn, B., Dahl, J.L., and Strominger, J.L (1971). GlycyltRNA synthetase (Sfaphy/ococcus aureus). Meth. Enzymol. 17, 966-970.
91. Ostrem, D.L., and Berg, P. (1970). Glycyl-tRNA synthetase: an oligomeric protein containing dissimilar subunits. Proc. Natl. Acad. Sei. USA 67,1967 -1974.
92. Ostrem, D.L., and Berg, P. (1974). Glycyl transfer ribonucleic acid synthetase from Escherichia coli: purification, properties and substrate binding. Biochemistry 73,1338-1348.
93. Fachmann, U., and Zachau, H.G. (1978). Yeast seryl tRNA synthetase: two sets of substrate sites involved in aminoacylation. Nucl. Acids Res. 5,961-973.
94. Pedersen, S., Bloch, P.L, Reeh, S., and Neidhardt, F.C. (1978). Patterns of protein synthesis in E coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell 14, 179-190.
95. Plateau, P., and Blanquet, S. (1994). Dinucleoside oligophosphates in micro-organisms. Adv. Microb. Physiol. 36,81 -109.
96. Poterszman, A., Delarue, M., Thierry, J.-C., and Moras, D. (1994). Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase. J. Mol. Biol. 244, 158-167.
97. Profy, AT., and Schimmel, P. (1986). A sulfhydryl presumed essential is not required for catalysis by an aminoacyl-tRNA synthetase. J. Biol. Chem. 267,15474 -15479.
98. Reeh, S., Pedersen, S., and Neidhardt, F.C. (1977). Transient rates of synthesis of five aminoacyl-transf er ribonucleic acid synthetases during a shift-up of Escherichia coli. J. Bacteriol. 729, 702-706.
99. Roback, E.R., Friesen, J.D., and Fill, N.P. (1973). A temperaturesensitive glycyl-transfer ribonucleic acid synthetase mutant of Escherichia coli. Can. J. Microbiol. 79,421 -426.
100. Roberts, J.W., and Carbon, J. (1975). Nucleotide sequence studies of normal and genetically altered glycine transfer ribonucleic acids from Escherichia coli. J. Biol. Chem. 250,5530 5541.
101. Roberts, W.K., and Olsen, M.L (1976). Studies on the formation and stability of aminoacyl-tRNA synthetase complexes from Ehrlich ascites cells. Biochim. Biophys. Acta 454,480 - 492.
102. Schimmel, P. (1991). Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. Trends Biochem. Sei. 76,1-3.
103. Schimmel, P., Keng, T., and Putney, S. (1982). Genes for two E coli aminoacyl-tRNA synthetases. Developments Biochem. 24, 49-56.
104. Shi, J.-P., Martinis, S.A., and Schimmel, P. (1992). RNA tetraloops as minimalist substrates for aminoacylation. Biochemistry 37, 4931-4936.
105. Shiba, K., Schimmel, P., Motegi, H., and Noda, T. (1994). Human glycyl-tRNA synthetase: wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J. Biol. Chem. 269,30049 - 30055.
106. Shimizu, M., Asahara, H.,Tamura, K., Hasegawa.T, and Himeno, H. (1992). The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases. J. Mol. Evol. 35,436 - 443; Erratum J.Mol.Evol.38,204(1994).
107. Soil, D., and Schimmel, P.R. (1974). Aminoacyl-tRNA synthetases. In: Enzymes, 3rd ed. P.D. Boyer, ed. (New York: Academic Press), pp. 489-538.
108. Southgate, C.C.B., and Dixon, H.B.F. (1978). Phosphonate analogues of aminoacyl adenylates. Biochem. J. 7 75,461 - 465.
109. Straus, D.S. (1974). Induction by mutagens of tandem gene duplications in the glyS region of the Escherichia coli chromosome. Genetics 78,823 - 830.
110. Straus, D.S., and D'Ari Straus, L. (1976). Large overlapping tandem genetic duplications in Salmonella typhimurium. J. Mol. Biol. 703,143-153.
111. Surguchev, A.R, and Surgucheva, I.G. (1974). Two forms of glycyl-tRNA synthetase from Bacillus brews. Biokhimiya 39, 1270-1277.
112. Surguchov, A.R, and Surguchova, I.G. (1975). Two enzymically active forms of glycyl-tRNA synthetase from Bacillus brevis: purification and properties. Eur. J. Biochem. 54,175 -184.
113. Suzuka, I., Tanaka, S., and Shimura, K. (1960). Amino acid incorporation enzyme in posterior silk gland. J. Biochem. 48, 774 776.
114. Suzuka, I., Tanaka, S., and Shimura, K. (1961). Amino acid activating enzyme free from pyrophosphate exchange. J. Biochem. 49,81-82.
115. Tanaka, S., Suzuka, I., and Shimura, K. (1962). Interaction of ATP with glycine activating enzyme. J. Biochem. 57,447 - 449.
116. Targoff, I.N. (1990). Autoantibodies to aminoacyl transfer RNA synthetases for isoleucine and glycine: two additional synthetases are antigenic in myositis. J. Immunol. 744,1737 -1743.
117. Targoff, I.N., Trieu, E.P., Plotz, P.M., and Miller, F.W. (1992). Antibodies to glycyl-transfer RNA synthetase in patients with myositis and interstitial lung disease. Arthritis Rheumatism 35, 821-830.
118. Toth, M.J., and Schimmel, R (1986). Internal structural features of E. coli glycyl-tRNA synthetase examined by subunit polypeptide chain fusions. J. Biol. Chem. 267,6643 - 6646.
119. Toth, M.J., and Schimmel, P. (1990a). Deletions in the large (beta) subunit of a hetero-oligomeric aminoacyl-tRNA synthetase. J. Biol. Chem. 265,1000 -1004.
120. Toth, M. J., and Schimmel, R (1990b). A mutation in the small (alpha) subunit of glycyl-tRNA synthetase affects amino acid activation and subunit association parameters. J. Biol. Chem. 265,1005-1009.
121. Wagar, E.A., Giese, M.J., Yasin, B., and Pang, M. (1995). The glycyl-tRNA synthetase of Chlamydia trachomatis. J. Bacteriol. 777,5179-5185.
122. Walker, E.J., Treacy, G.B., and Jeffrey, P.D. (1983). Molecular weights of mitochondria! and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes. Biochemistry 22,1934-1941.
123. Webster, T.A., Gibson, B.W., Keng, T., Biemann, K., and Schimmel, P. (1983). Primary structures of both subunits of £co//glycyl-tRNA synthetase. J. Biol. Chem. 258,10637 -10641.
124. Williams, J., Osvath, S., Khong, T.F., Pearse, M., and Power, D. (1995). Cloning, sequencing and bacterial expression of human glycine tRNA synthetase. Nucl. Acids Res. 23, 1307 1310.
125. Wright, H.T., Nurse, K.C., and Goldstein, D.J. (1981). Nalidixic acid, oxolinic acid, and novobiocin inhibit yeast glycyl- and leucyl-tRNA synthetases. Science 273,455 - 456.
126. Wu, H., Nada, S., and Dignam, D. (1995). Analysis of truncated forms of Bombyx mon glycyl-tRNA synthetase: function of an N-terminal structure in RNA binding. Biochemistry 34,16327 16336.