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Volumn 367, Issue 4, 2007, Pages 1063-1078

Kinetic Quality Control of Anticodon Recognition by a Eukaryotic Aminoacyl-tRNA Synthetase

Author keywords

burst kinetics; cysteinyl tRNA synthetase; induced fit; product release; transient kinetics

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; CYSTEINE TRANSFER RNA; PROTEIN CYSRS; UNCLASSIFIED DRUG;

EID: 33847716306     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.050     Document Type: Article
Times cited : (25)

References (55)
  • 1
    • 0015378783 scopus 로고
    • The frequency of errors in protein biosynthesis
    • Loftfield R.B., and Vanderjagt D. The frequency of errors in protein biosynthesis. Biochem. J. 128 (1972) 1353-1356
    • (1972) Biochem. J. , vol.128 , pp. 1353-1356
    • Loftfield, R.B.1    Vanderjagt, D.2
  • 2
    • 0013019697 scopus 로고    scopus 로고
    • Ibba M., Francklyn C., and Cusack S. (Eds), Landes Bioscience, Georgetown, Texas
    • Ibba M., Francklyn C., and Cusack S. In: Ibba M., Francklyn C., and Cusack S. (Eds). The Aminoacyl-tRNA Synthetases (2005), Landes Bioscience, Georgetown, Texas
    • (2005) The Aminoacyl-tRNA Synthetases
    • Ibba, M.1    Francklyn, C.2    Cusack, S.3
  • 4
    • 0032562707 scopus 로고    scopus 로고
    • Sieves in sequence
    • Fersht A.R. Sieves in sequence. Science 280 (1998) 541
    • (1998) Science , vol.280 , pp. 541
    • Fersht, A.R.1
  • 5
    • 33645135634 scopus 로고    scopus 로고
    • Multi-aminoacyl-tRNA synthetase complexes
    • Ibba M., Francklyn C., and Cusack S. (Eds), Landes Bioscience, Georgetown, Texas
    • Mirande M. Multi-aminoacyl-tRNA synthetase complexes. In: Ibba M., Francklyn C., and Cusack S. (Eds). The Aminoacyl-tRNA Synthetases (2005), Landes Bioscience, Georgetown, Texas 298-308
    • (2005) The Aminoacyl-tRNA Synthetases , pp. 298-308
    • Mirande, M.1
  • 6
    • 33644668804 scopus 로고    scopus 로고
    • A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins
    • Wolfe C.L., Warrington J.A., Treadwell L., and Norcum M.T. A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins. J. Biol. Chem. 280 (2005) 38870-3888
    • (2005) J. Biol. Chem. , vol.280 , pp. 38870-33888
    • Wolfe, C.L.1    Warrington, J.A.2    Treadwell, L.3    Norcum, M.T.4
  • 7
    • 25144489447 scopus 로고    scopus 로고
    • Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers
    • Park S.G., Ewalt K.L., and Kim S. Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem. Sci. 30 (2005) 569-574
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 569-574
    • Park, S.G.1    Ewalt, K.L.2    Kim, S.3
  • 9
    • 0037127205 scopus 로고    scopus 로고
    • The N-terminal domain of mammalian lysyl-tRNA synthetase is a functional tRNA-binding domain
    • Francin M., Kaminska M., Kerjan P., and Mirande M. The N-terminal domain of mammalian lysyl-tRNA synthetase is a functional tRNA-binding domain. J. Biol. Chem. 277 (2002) 1762-1769
    • (2002) J. Biol. Chem. , vol.277 , pp. 1762-1769
    • Francin, M.1    Kaminska, M.2    Kerjan, P.3    Mirande, M.4
  • 10
    • 0034141480 scopus 로고    scopus 로고
    • A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases
    • Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., and Mirande M. A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J. 19 (2000) 445-452
    • (2000) EMBO J. , vol.19 , pp. 445-452
    • Cahuzac, B.1    Berthonneau, E.2    Birlirakis, N.3    Guittet, E.4    Mirande, M.5
  • 11
    • 0035960596 scopus 로고    scopus 로고
    • The appended C-domain of human methionyl-tRNA synthetase has a tRNA- sequestering function
    • Kaminska M., Shalak V., and Mirande M. The appended C-domain of human methionyl-tRNA synthetase has a tRNA- sequestering function. Biochemistry 40 (2001) 14309-14316
    • (2001) Biochemistry , vol.40 , pp. 14309-14316
    • Kaminska, M.1    Shalak, V.2    Mirande, M.3
  • 12
    • 0034671360 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly
    • Robinson J.C., Kerjan P., and Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly. J. Mol. Biol. 304 (2000) 983-994
    • (2000) J. Mol. Biol. , vol.304 , pp. 983-994
    • Robinson, J.C.1    Kerjan, P.2    Mirande, M.3
  • 14
    • 27144445976 scopus 로고    scopus 로고
    • The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
    • Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., and Wang E.D. The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. J. Biol. Chem. 280 (2005) 34755-34763
    • (2005) J. Biol. Chem. , vol.280 , pp. 34755-34763
    • Ling, C.1    Yao, Y.N.2    Zheng, Y.G.3    Wei, H.4    Wang, L.5    Wu, X.F.6    Wang, E.D.7
  • 15
    • 0020359763 scopus 로고
    • Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit
    • Mirande M., Kellermann O., and Waller J.P. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit. J. Biol. Chem. 257 (1982) 11049-11055
    • (1982) J. Biol. Chem. , vol.257 , pp. 11049-11055
    • Mirande, M.1    Kellermann, O.2    Waller, J.P.3
  • 16
    • 0028108750 scopus 로고
    • Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit
    • Shiba K., Suzuki N., Shigesada K., Namba Y., Schimmel P., and Noda T. Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc. Natl Acad. Sci. USA 91 (1994) 7435-7439
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7435-7439
    • Shiba, K.1    Suzuki, N.2    Shigesada, K.3    Namba, Y.4    Schimmel, P.5    Noda, T.6
  • 17
    • 0027983773 scopus 로고
    • A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope
    • Raben N., Nichols R., Dohlman J., McPhie P., Sridhar V., Hyde C., et al. A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J. Biol. Chem. 269 (1994) 24277-24283
    • (1994) J. Biol. Chem. , vol.269 , pp. 24277-24283
    • Raben, N.1    Nichols, R.2    Dohlman, J.3    McPhie, P.4    Sridhar, V.5    Hyde, C.6
  • 18
    • 0035040785 scopus 로고    scopus 로고
    • Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl- tRNA synthetase
    • Davidson E., Caffarella J., Vitseva O., Hou Y.M., and King M.P. Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl- tRNA synthetase. Biol. Chem. 382 (2001) 399-406
    • (2001) Biol. Chem. , vol.382 , pp. 399-406
    • Davidson, E.1    Caffarella, J.2    Vitseva, O.3    Hou, Y.M.4    King, M.P.5
  • 19
    • 0037013921 scopus 로고    scopus 로고
    • Structural origins of amino acid selection without editing by cysteinyl- tRNA synthetase
    • Newberry K.J., Hou Y.M., and Perona J.J. Structural origins of amino acid selection without editing by cysteinyl- tRNA synthetase. EMBO J. 21 (2002) 2778-2787
    • (2002) EMBO J. , vol.21 , pp. 2778-2787
    • Newberry, K.J.1    Hou, Y.M.2    Perona, J.J.3
  • 21
    • 0027291262 scopus 로고
    • Recognition of tRNA(Cys) by Escherichia coli cysteinyl-tRNA synthetase
    • (Published erratum appears in Biochemistry (1993).32:13374)
    • Komatsoulis G.A., and Abelson J. Recognition of tRNA(Cys) by Escherichia coli cysteinyl-tRNA synthetase. Biochemistry 32 (1993) 7435-7444 (Published erratum appears in Biochemistry (1993).32:13374)
    • (1993) Biochemistry , vol.32 , pp. 7435-7444
    • Komatsoulis, G.A.1    Abelson, J.2
  • 22
    • 0032506221 scopus 로고    scopus 로고
    • Aminoacylation of tRNA in the evolution of an aminoacyl-tRNA synthetase
    • Lipman R.S., and Hou Y.M. Aminoacylation of tRNA in the evolution of an aminoacyl-tRNA synthetase. Proc. Natl Acad. Sci. USA 95 (1998) 13495-13500
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13495-13500
    • Lipman, R.S.1    Hou, Y.M.2
  • 24
    • 0027313443 scopus 로고
    • An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA
    • Hou Y.M., Westhof E., and Giege R. An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA. Proc. Natl Acad. Sci. USA 90 (1993) 6776-6780
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6776-6780
    • Hou, Y.M.1    Westhof, E.2    Giege, R.3
  • 25
    • 0031404731 scopus 로고    scopus 로고
    • Cysteinyl-tRNA synthetase from Saccharomyces cerevisiae. Purification, characterization and assignment to the genomic sequence YNL247w
    • Motorin Y., Le Caer J.P., and Waller J.P. Cysteinyl-tRNA synthetase from Saccharomyces cerevisiae. Purification, characterization and assignment to the genomic sequence YNL247w. Biochimie 79 (1997) 731-740
    • (1997) Biochimie , vol.79 , pp. 731-740
    • Motorin, Y.1    Le Caer, J.P.2    Waller, J.P.3
  • 26
    • 0032463934 scopus 로고    scopus 로고
    • Purification and properties of cysteinyl-tRNA synthetase from rabbit liver
    • Motorin Y., and Waller J.P. Purification and properties of cysteinyl-tRNA synthetase from rabbit liver. Biochimie 80 (1998) 579-590
    • (1998) Biochimie , vol.80 , pp. 579-590
    • Motorin, Y.1    Waller, J.P.2
  • 27
    • 18544382985 scopus 로고    scopus 로고
    • Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity
    • Zhang C.M., and Hou Y.M. Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity. Biochemistry 44 (2005) 7240-7249
    • (2005) Biochemistry , vol.44 , pp. 7240-7249
    • Zhang, C.M.1    Hou, Y.M.2
  • 28
    • 0037099498 scopus 로고    scopus 로고
    • Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition
    • Yaremchuk A., Kriklivyi I., Tukalo M., and Cusack S. Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J. 21 (2002) 3829-3840
    • (2002) EMBO J. , vol.21 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 29
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublie S., Bricogne G., Gilmore C., and Carter Jr. C.W. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 3 (1995) 17-31
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublie, S.1    Bricogne, G.2    Gilmore, C.3    Carter Jr., C.W.4
  • 30
    • 33745529250 scopus 로고    scopus 로고
    • Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis
    • Yang X.L., Otero F.J., Ewalt K.L., Liu J., Swairjo M.A., Kohrer C., et al. Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. EMBO J. 25 (2006) 2919-2929
    • (2006) EMBO J. , vol.25 , pp. 2919-2929
    • Yang, X.L.1    Otero, F.J.2    Ewalt, K.L.3    Liu, J.4    Swairjo, M.A.5    Kohrer, C.6
  • 32
    • 0038408635 scopus 로고    scopus 로고
    • Association of an aminoacyl-tRNA synthetase with a putative metabolic Ppotein in Archaea
    • Lipman R.S., Chen J., Evilia C., Vitseva O., and Hou Y.M. Association of an aminoacyl-tRNA synthetase with a putative metabolic Ppotein in Archaea. Biochemistry 42 (2003) 7487-7496
    • (2003) Biochemistry , vol.42 , pp. 7487-7496
    • Lipman, R.S.1    Chen, J.2    Evilia, C.3    Vitseva, O.4    Hou, Y.M.5
  • 33
    • 0033550073 scopus 로고    scopus 로고
    • tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase
    • Bovee M.L., Yan W., Sproat B.S., and Francklyn C.S. tRNA discrimination at the binding step by a class II aminoacyl-tRNA synthetase. Biochemistry 38 (1999) 13725-13735
    • (1999) Biochemistry , vol.38 , pp. 13725-13735
    • Bovee, M.L.1    Yan, W.2    Sproat, B.S.3    Francklyn, C.S.4
  • 34
    • 0141653988 scopus 로고    scopus 로고
    • Amino acid discrimination by a highly differentiated metal center of an aminoacyl-tRNA synthetase
    • Zhang C.M., Perona J.J., and Hou Y.M. Amino acid discrimination by a highly differentiated metal center of an aminoacyl-tRNA synthetase. Biochemistry 42 (2003) 10931-10937
    • (2003) Biochemistry , vol.42 , pp. 10931-10937
    • Zhang, C.M.1    Perona, J.J.2    Hou, Y.M.3
  • 35
    • 5144223811 scopus 로고    scopus 로고
    • Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics
    • Uter N.T., and Perona J.J. Long-range intramolecular signaling in a tRNA synthetase complex revealed by pre-steady-state kinetics. Proc. Natl Acad. Sci. USA 101 (2004) 14396-41401
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14396-41401
    • Uter, N.T.1    Perona, J.J.2
  • 36
    • 33746189733 scopus 로고    scopus 로고
    • Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases
    • Zhang C.M., Perona J.J., Ryu K., Francklyn C., and Hou Y.M. Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases. J. Mol. Biol. 361 (2006) 300-311
    • (2006) J. Mol. Biol. , vol.361 , pp. 300-311
    • Zhang, C.M.1    Perona, J.J.2    Ryu, K.3    Francklyn, C.4    Hou, Y.M.5
  • 37
    • 21244444325 scopus 로고    scopus 로고
    • Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase
    • Uter N.T., Gruic-Sovulj I., and Perona J.J. Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase. J. Biol. Chem. 280 (2005) 23966-23977
    • (2005) J. Biol. Chem. , vol.280 , pp. 23966-23977
    • Uter, N.T.1    Gruic-Sovulj, I.2    Perona, J.J.3
  • 38
    • 0642315208 scopus 로고
    • Transient state kinetic analysis of enzyme reaction pathways
    • Johnson K.A. Transient state kinetic analysis of enzyme reaction pathways. The Enzymes 20 (1992) 1-61
    • (1992) The Enzymes , vol.20 , pp. 1-61
    • Johnson, K.A.1
  • 39
    • 0029004348 scopus 로고
    • Enzymatic aminoacylation of tRNA acceptor stem helices with cysteine is dependent on a single nucleotide
    • Hamann C.S., and Hou Y.M. Enzymatic aminoacylation of tRNA acceptor stem helices with cysteine is dependent on a single nucleotide. Biochemistry 34 (1995) 6527-6532
    • (1995) Biochemistry , vol.34 , pp. 6527-6532
    • Hamann, C.S.1    Hou, Y.M.2
  • 40
    • 0034923932 scopus 로고    scopus 로고
    • Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms
    • Rodnina M.V., and Wintermeyer W. Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms. Annu. Rev. Biochem. 70 (2001) 415-435
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 415-435
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 41
    • 0034658247 scopus 로고    scopus 로고
    • A domain in the N-terminal extension of class IIb eukaryotic aminoacyl- tRNA synthetases is important for tRNA binding
    • Frugier M., Moulinier L., and Giege R. A domain in the N-terminal extension of class IIb eukaryotic aminoacyl- tRNA synthetases is important for tRNA binding. EMBO J. 19 (2000) 2371-2380
    • (2000) EMBO J. , vol.19 , pp. 2371-2380
    • Frugier, M.1    Moulinier, L.2    Giege, R.3
  • 42
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y., Gojobori T., and Ikemura T. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucl. Acids Res. 28 (2000) 292
    • (2000) Nucl. Acids Res. , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 43
    • 0024416460 scopus 로고
    • Mechanisms of aminoacyl-tRNA synthetases: a critical consideration of recent results
    • Freist W. Mechanisms of aminoacyl-tRNA synthetases: a critical consideration of recent results. Biochemistry 28 (1989) 6787-6795
    • (1989) Biochemistry , vol.28 , pp. 6787-6795
    • Freist, W.1
  • 44
    • 0029078593 scopus 로고
    • Proofreading in vivo. Editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli
    • Jakubowski H. Proofreading in vivo. Editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli. J. Biol. Chem. 270 (1995) 17672-17673
    • (1995) J. Biol. Chem. , vol.270 , pp. 17672-17673
    • Jakubowski, H.1
  • 45
    • 0014027087 scopus 로고
    • Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
    • Baldwin A.N., and Berg P. Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase. J. Biol. Chem. 241 (1966) 839-845
    • (1966) J. Biol. Chem. , vol.241 , pp. 839-845
    • Baldwin, A.N.1    Berg, P.2
  • 46
    • 0028305036 scopus 로고
    • Mutational isolation of a sieve for editing in a transfer RNA synthetase
    • Schmidt E., and Schimmel P. Mutational isolation of a sieve for editing in a transfer RNA synthetase. Science 264 (1994) 265-267
    • (1994) Science , vol.264 , pp. 265-267
    • Schmidt, E.1    Schimmel, P.2
  • 47
    • 12844282196 scopus 로고    scopus 로고
    • Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase
    • Swairjo M.A., and Schimmel P.R. Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase. Proc. Natl Acad. Sci. USA 102 (2005) 988-993
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 988-993
    • Swairjo, M.A.1    Schimmel, P.R.2
  • 48
    • 33644677385 scopus 로고    scopus 로고
    • Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase
    • Roy H., Ling J., Alfonzo J., and Ibba M. Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. J. Biol. Chem. 280 (2005) 38186-38192
    • (2005) J. Biol. Chem. , vol.280 , pp. 38186-38192
    • Roy, H.1    Ling, J.2    Alfonzo, J.3    Ibba, M.4
  • 49
    • 8644231651 scopus 로고    scopus 로고
    • Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution
    • Dock-Bregeon A.C., Rees B., Torres-Larios A., Bey G., Caillet J., and Moras D. Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. Mol. Cell 16 (2004) 375-386
    • (2004) Mol. Cell , vol.16 , pp. 375-386
    • Dock-Bregeon, A.C.1    Rees, B.2    Torres-Larios, A.3    Bey, G.4    Caillet, J.5    Moras, D.6
  • 51
    • 0347993060 scopus 로고    scopus 로고
    • An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing
    • Wong F.C., Beuning P.J., Silvers C., and Musier-Forsyth K. An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing. J. Biol. Chem. 278 (2003) 52857-52864
    • (2003) J. Biol. Chem. , vol.278 , pp. 52857-52864
    • Wong, F.C.1    Beuning, P.J.2    Silvers, C.3    Musier-Forsyth, K.4
  • 52
    • 9344262901 scopus 로고    scopus 로고
    • Tyr deacylase for editing in Thr-tRNA synthetase
    • Tyr deacylase for editing in Thr-tRNA synthetase. RNA 10 (2004) 1845-1851
    • (2004) RNA , vol.10 , pp. 1845-1851
    • Rigden, D.J.1
  • 53
    • 0016437581 scopus 로고
    • Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases
    • Fersht A.R., Ashford J.S., Bruton C.J., Jakes R., Koch G.L., and Hartley B.S. Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases. Biochemistry 14 (1975) 1-4
    • (1975) Biochemistry , vol.14 , pp. 1-4
    • Fersht, A.R.1    Ashford, J.S.2    Bruton, C.J.3    Jakes, R.4    Koch, G.L.5    Hartley, B.S.6
  • 54
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew E., and Williams K. Determination of molecular masses of proteins in solution: implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Techniqs 10 (1999) 51-63
    • (1999) J. Biomol. Techniqs , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.2
  • 55
    • 14844357908 scopus 로고    scopus 로고
    • A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase
    • Guth E., Connolly S.H., Bovee M., and Francklyn C.S. A substrate-assisted concerted mechanism for aminoacylation by a class II aminoacyl-tRNA synthetase. Biochemistry 44 (2005) 3785-3794
    • (2005) Biochemistry , vol.44 , pp. 3785-3794
    • Guth, E.1    Connolly, S.H.2    Bovee, M.3    Francklyn, C.S.4


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