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Volumn 581, Issue 16, 2007, Pages 2959-2964

Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy

Author keywords

GARS; Motor neuron; SMA

Indexed keywords

GLYCINE; GLYCINE TRANSFER RNA LIGASE; TRANSFER RNA;

EID: 34250340882     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.046     Document Type: Article
Times cited : (31)

References (34)
  • 1
    • 0032005233 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase from Thermus thermophilus - wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems
    • Mazauric M.H., Keith G., Logan D., Kreutzer R., Giege R., and Kern D. Glycyl-tRNA synthetase from Thermus thermophilus - wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems. Eur. J. Biochem. 251 (1998) 744-757
    • (1998) Eur. J. Biochem. , vol.251 , pp. 744-757
    • Mazauric, M.H.1    Keith, G.2    Logan, D.3    Kreutzer, R.4    Giege, R.5    Kern, D.6
  • 2
    • 14244262599 scopus 로고    scopus 로고
    • Evolution of different oligomeric glycyl-tRNA synthetases
    • Tang S.N., and Huang J.F. Evolution of different oligomeric glycyl-tRNA synthetases. FEBS Lett. 579 (2005) 1441-1445
    • (2005) FEBS Lett. , vol.579 , pp. 1441-1445
    • Tang, S.N.1    Huang, J.F.2
  • 3
    • 0030756651 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases in biology and disease: new evidence for structural and functional diversity in an ancient family of enzymes
    • Francklyn C., Musier-Forsyth K., and Martinis S.A. Aminoacyl-tRNA synthetases in biology and disease: new evidence for structural and functional diversity in an ancient family of enzymes. RNA 3 (1997) 954-960
    • (1997) RNA , vol.3 , pp. 954-960
    • Francklyn, C.1    Musier-Forsyth, K.2    Martinis, S.A.3
  • 5
    • 0038067742 scopus 로고    scopus 로고
    • Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V
    • Antonellis A., et al. Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. Am. J. Hum. Genet. 72 (2003) 1293-1299
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1293-1299
    • Antonellis, A.1
  • 6
    • 0032569930 scopus 로고    scopus 로고
    • Autosomal dominant distal spinal muscular atrophy type V (dSMA-V) and Charcot-Marie-Tooth disease type 2D (CMT2D) segregate within a single large kindred and map to a refined region on chromosome 7p15
    • Sambuughin N., Sivakumar K., Selenge B., Lee H.S., Friedlich D., Baasanjav D., Dalakas M.C., and Goldfarb L.G. Autosomal dominant distal spinal muscular atrophy type V (dSMA-V) and Charcot-Marie-Tooth disease type 2D (CMT2D) segregate within a single large kindred and map to a refined region on chromosome 7p15. J. Neurol. Sci. 161 (1998) 23-28
    • (1998) J. Neurol. Sci. , vol.161 , pp. 23-28
    • Sambuughin, N.1    Sivakumar, K.2    Selenge, B.3    Lee, H.S.4    Friedlich, D.5    Baasanjav, D.6    Dalakas, M.C.7    Goldfarb, L.G.8
  • 7
    • 0029145426 scopus 로고
    • Mapping of a distal form of spinal muscular atrophy with upper limb predominance to chromosome 7p
    • Christodoulou K., et al. Mapping of a distal form of spinal muscular atrophy with upper limb predominance to chromosome 7p. Hum. Mol. Genet. 4 (1995) 1629-1632
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1629-1632
    • Christodoulou, K.1
  • 8
    • 0031215415 scopus 로고    scopus 로고
    • Confirmation of a second locus for CMT2 and evidence for additional genetic heterogeneity
    • Pericak-Vance M.A., et al. Confirmation of a second locus for CMT2 and evidence for additional genetic heterogeneity. Neurogenetics 1 (1997) 89-93
    • (1997) Neurogenetics , vol.1 , pp. 89-93
    • Pericak-Vance, M.A.1
  • 9
    • 26044454330 scopus 로고    scopus 로고
    • Phenotypic spectrum of disorders associated with glycyl-tRNA synthetase mutations
    • Sivakumar K., et al. Phenotypic spectrum of disorders associated with glycyl-tRNA synthetase mutations. Brain 128 (2005) 2304-2314
    • (2005) Brain , vol.128 , pp. 2304-2314
    • Sivakumar, K.1
  • 10
    • 33745664558 scopus 로고    scopus 로고
    • The G526R glycyl-tRNA synthetase gene mutation in distal hereditary motor neuropathy type V
    • Dubourg O., et al. The G526R glycyl-tRNA synthetase gene mutation in distal hereditary motor neuropathy type V. Neurology 66 (2006) 1721-1726
    • (2006) Neurology , vol.66 , pp. 1721-1726
    • Dubourg, O.1
  • 11
    • 33645884424 scopus 로고    scopus 로고
    • Coexistence of CMT-2D and distal SMA-V phenotypes in an Italian family with a GARS gene mutation
    • Del Bo R., et al. Coexistence of CMT-2D and distal SMA-V phenotypes in an Italian family with a GARS gene mutation. Neurology 66 (2006) 752-754
    • (2006) Neurology , vol.66 , pp. 752-754
    • Del Bo, R.1
  • 12
    • 33751001764 scopus 로고    scopus 로고
    • Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene
    • James P.A., Cader M.Z., Muntoni F., Childs A.M., Crow Y.J., and Talbot K. Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene. Neurology 67 (2006) 1710-1712
    • (2006) Neurology , vol.67 , pp. 1710-1712
    • James, P.A.1    Cader, M.Z.2    Muntoni, F.3    Childs, A.M.4    Crow, Y.J.5    Talbot, K.6
  • 13
    • 31744448271 scopus 로고    scopus 로고
    • Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
    • Jordanova A., et al. Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat. Genet. 38 (2006) 197-202
    • (2006) Nat. Genet. , vol.38 , pp. 197-202
    • Jordanova, A.1
  • 14
    • 33748432548 scopus 로고    scopus 로고
    • Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
    • Lee J.W., et al. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration. Nature 443 (2006) 50-55
    • (2006) Nature , vol.443 , pp. 50-55
    • Lee, J.W.1
  • 15
    • 23844515485 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization
    • Walter T.S., et al. A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization. Acta Crystallogr. D Biol. Crystallogr. 61 (2005) 651-657
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 651-657
    • Walter, T.S.1
  • 16
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 Pt 2 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: a new software suite for macromolecular structure determination
    • Brunger A.T., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 19
    • 0029091055 scopus 로고
    • Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
    • Logan D.T., Mazauric M.H., Kern D., and Moras D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. EMBO J. 14 (1995) 4156-4167
    • (1995) EMBO J. , vol.14 , pp. 4156-4167
    • Logan, D.T.1    Mazauric, M.H.2    Kern, D.3    Moras, D.4
  • 20
    • 0027942420 scopus 로고
    • Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation
    • Shiba K., Schimmel P., Motegi H., and Noda T. Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J. Biol. Chem. 269 (1994) 30049-30055
    • (1994) J. Biol. Chem. , vol.269 , pp. 30049-30055
    • Shiba, K.1    Schimmel, P.2    Motegi, H.3    Noda, T.4
  • 21
    • 0000983324 scopus 로고    scopus 로고
    • Interaction between human tRNA synthetases involves repeated sequence elements
    • Rho S.B., Lee K.H., Kim J.W., Shiba K., Jo Y.J., and Kim S. Interaction between human tRNA synthetases involves repeated sequence elements. Proc. Natl. Acad. Sci. USA 93 (1996) 10128-10133
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10128-10133
    • Rho, S.B.1    Lee, K.H.2    Kim, J.W.3    Shiba, K.4    Jo, Y.J.5    Kim, S.6
  • 22
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G., Delarue M., Poch O., Gangloff J., and Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347 (1990) 203-206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 24
    • 0035101674 scopus 로고    scopus 로고
    • Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer
    • Carrodeguas J.A., Theis K., Bogenhagen D.F., and Kisker C. Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer. Mol. Cell 7 (2001) 43-54
    • (2001) Mol. Cell , vol.7 , pp. 43-54
    • Carrodeguas, J.A.1    Theis, K.2    Bogenhagen, D.F.3    Kisker, C.4
  • 25
    • 0033617335 scopus 로고    scopus 로고
    • The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
    • Sankaranarayanan R., et al. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97 (1999) 371-381
    • (1999) Cell , vol.97 , pp. 371-381
    • Sankaranarayanan, R.1
  • 26
    • 0033548581 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    • Arnez J.G., Dock-Bregeon A.C., and Moras D. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. J. Mol. Biol. 286 (1999) 1449-1459
    • (1999) J. Mol. Biol. , vol.286 , pp. 1449-1459
    • Arnez, J.G.1    Dock-Bregeon, A.C.2    Moras, D.3
  • 27
    • 33845474123 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease
    • Xie W., Schimmel P., and Yang X.L. Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1243-1246
    • (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.62 , pp. 1243-1246
    • Xie, W.1    Schimmel, P.2    Yang, X.L.3
  • 28
    • 11544277817 scopus 로고    scopus 로고
    • 3'-Azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes
    • Ren J., et al. 3'-Azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes. Proc. Natl. Acad. Sci. USA 95 (1998) 9518-9523
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9518-9523
    • Ren, J.1
  • 29
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer G.J., Patten P.A., Wang L.H., Schultz P.G., and Stevens R.C. Structural insights into the evolution of an antibody combining site. Science 276 (1997) 1665-1669
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 30
    • 0034282792 scopus 로고    scopus 로고
    • Crystal structure of a eukaryote/archaeon-like protyl-tRNA synthetase and its complex with tRNAPro(CGG)
    • Yaremchuk A., Cusack S., and Tukalo M. Crystal structure of a eukaryote/archaeon-like protyl-tRNA synthetase and its complex with tRNAPro(CGG). EMBO J. 19 (2000) 4745-4758
    • (2000) EMBO J. , vol.19 , pp. 4745-4758
    • Yaremchuk, A.1    Cusack, S.2    Tukalo, M.3
  • 31
    • 0037881907 scopus 로고    scopus 로고
    • Thermodynamic characterization of the binding of nucleotides to glycyl-tRNA synthetase
    • Dignam J.D., Nada S., and Chaires J.B. Thermodynamic characterization of the binding of nucleotides to glycyl-tRNA synthetase. Biochemistry 42 (2003) 5333-5340
    • (2003) Biochemistry , vol.42 , pp. 5333-5340
    • Dignam, J.D.1    Nada, S.2    Chaires, J.B.3
  • 32
    • 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) 14396-14401
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14396-14401
    • Uter, N.T.1    Perona, J.J.2
  • 33
    • 0019873835 scopus 로고
    • Glycyl-tRNA synthetase from baker's yeast. Interconversion between active and inactive forms of the enzyme
    • Kern D., Giege R., and Ebel J.P. Glycyl-tRNA synthetase from baker's yeast. Interconversion between active and inactive forms of the enzyme. Biochemistry 20 (1981) 122-131
    • (1981) Biochemistry , vol.20 , pp. 122-131
    • Kern, D.1    Giege, R.2    Ebel, J.P.3
  • 34
    • 33748545328 scopus 로고    scopus 로고
    • An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D
    • Seburn K.L., Nangle L.A., Cox G.A., Schimmel P., and Burgess R.W. An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D. Mouse Model Neuron 51 (2006) 715-726
    • (2006) Mouse Model Neuron , vol.51 , pp. 715-726
    • Seburn, K.L.1    Nangle, L.A.2    Cox, G.A.3    Schimmel, P.4    Burgess, R.W.5


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