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Volumn 19, Issue 10, 2000, Pages 2371-2380

A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding

Author keywords

Aminoacyl tRNA synthetase; Aspartyl tRNA synthetase; RNA binding motif; Synthetase extension

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; TRANSFER RNA;

EID: 0034658247     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.10.2371     Document Type: Article
Times cited : (86)

References (49)
  • 1
    • 0028988414 scopus 로고
    • Polyanion-induced α-helical structure of a synthetic 23-residue peptide representing the lysine-rich segment of the N-terminal extension of yeast cytoplasmic aspartyl-tRNA synthetase
    • Agou, F., Yang, Y., Gesquière, J.-C., Waller, J.-P. and Guittet, E. (1995) Polyanion-induced α-helical structure of a synthetic 23-residue peptide representing the lysine-rich segment of the N-terminal extension of yeast cytoplasmic aspartyl-tRNA synthetase. Biochemistry, 34, 569-576.
    • (1995) Biochemistry , vol.34 , pp. 569-576
    • Agou, F.1    Yang, Y.2    Gesquière, J.-C.3    Waller, J.-P.4    Guittet, E.5
  • 2
    • 0029828910 scopus 로고    scopus 로고
    • 2-terminal polypeptide extension on enzyme activity and stability
    • 2-terminal polypeptide extension on enzyme activity and stability. J. Biol. Chem., 271, 29295-29303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29295-29303
    • Agou, F.1    Waller, J.-P.2    Mirande, M.3
  • 3
    • 0030811296 scopus 로고    scopus 로고
    • Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes
    • Becker, H.D., Reinbolt, J., Kreutzer, R., Giegé, R. and Kern, D. (1997) Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes. Biochemistry, 36, 8785-8797.
    • (1997) Biochemistry , vol.36 , pp. 8785-8797
    • Becker, H.D.1    Reinbolt, J.2    Kreutzer, R.3    Giegé, R.4    Kern, D.5
  • 5
    • 0023019586 scopus 로고
    • High-level overexpression, rapid purification, and properties of escherichia coli tRNA nucleotidyltransferase
    • Cudny, H. and Deutscher, M.P. (1986) High-level overexpression, rapid purification, and properties of Escherichia coli tRNA nucleotidyltransferase. J. Biol. Chem., 261, 6450-6453.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6450-6453
    • Cudny, H.1    Deutscher, M.P.2
  • 6
    • 0027674975 scopus 로고
    • The aminoacyl-tRNA synthetases family: Modules at work
    • Delarue, M. and Moras, D. (1993) The aminoacyl-tRNA synthetases family: modules at work. BioEssays, 15, 675-687.
    • (1993) BioEssays , vol.15 , pp. 675-687
    • Delarue, M.1    Moras, D.2
  • 7
    • 0017380076 scopus 로고
    • Mapping adenines, guanines and pyrimidines in RNA
    • Donis-Keller, H., Maxam, A.M. and Gilbert, W. (1977) Mapping adenines, guanines and pyrimidines in RNA. Nucleic Acids Res., 4, 2527-2538.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 2527-2538
    • Donis-Keller, H.1    Maxam, A.M.2    Gilbert, W.3
  • 8
    • 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. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 9
    • 0025916062 scopus 로고
    • Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organization by deletion analysis
    • Eriani, G., Prevost, G., Kern, D., Vincendon, P., Dirheimer, G. and Gangloff, J. (1991) Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organization by deletion analysis. Eur. J. Biochem., 200, 337-343.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 337-343
    • Eriani, G.1    Prevost, G.2    Kern, D.3    Vincendon, P.4    Dirheimer, G.5    Gangloff, J.6
  • 10
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional model representations of macromolecules
    • Evans, S. (1993) SETOR: hardware lighted three-dimensional model representations of macromolecules. J. Mol. Graph., 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.1
  • 11
    • 0019883175 scopus 로고
    • Partial digestion of tRNA-aminoacyl-tRNA synthetase complexes with cobra venom ribonuclease
    • Favorova, O.O., Fasiolo, F., Keith, G., Vassilenko, S.K. and Ebel, J.-P. (1981) Partial digestion of tRNA-aminoacyl-tRNA synthetase complexes with cobra venom ribonuclease. Biochemistry, 20, 1006-1011.
    • (1981) Biochemistry , vol.20 , pp. 1006-1011
    • Favorova, O.O.1    Fasiolo, F.2    Keith, G.3    Vassilenko, S.K.4    Ebel, J.-P.5
  • 12
    • 0025056629 scopus 로고
    • Asp and interaction of this tRNA with yeast aspartyl-tRNA synthetase
    • Asp and interaction of this tRNA with yeast aspartyl-tRNA synthetase. Nucleic Acids Res., 18, 89-95.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 89-95
    • Garcia, A.1    Giegé, R.2    Behr, J.-P.3
  • 13
    • 0019197641 scopus 로고
    • Cristallisation du complexe formé entre l'aspartate-tRNA de levure et son aminoacyl-tRNA synthétase spécifique
    • Giegé, R., Lorber, B., Ebel, J.-P., Moras, D. and Thierry, J.-C. (1980) Cristallisation du complexe formé entre l'aspartate-tRNA de levure et son aminoacyl-tRNA synthétase spécifique. C.R. Acad. Sci. Paris D-2, 291, 393-396.
    • (1980) C.R. Acad. Sci. Paris D-2 , vol.291 , pp. 393-396
    • Giegé, R.1    Lorber, B.2    Ebel, J.-P.3    Moras, D.4    Thierry, J.-C.5
  • 15
    • 0003352234 scopus 로고    scopus 로고
    • Chemical and enzymatic probing of RNA structure
    • Barton, D.H.R. and Nakanishi, K. (eds), Pergamon, Oxford, UK
    • Giegé, R., Helm, M. and Florentz, C. (1999) Chemical and enzymatic probing of RNA structure. In Barton, D.H.R. and Nakanishi, K. (eds), Comprehensive Natural Product Chemistry. Pergamon, Oxford, UK, Vol. 6, pp. 63-80.
    • (1999) Comprehensive Natural Product Chemistry , vol.6 , pp. 63-80
    • Giegé, R.1    Helm, M.2    Florentz, C.3
  • 16
    • 0030908418 scopus 로고    scopus 로고
    • Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase
    • Glasfeld, E. and Schimmel, P. (1997) Zinc-dependent tRNA binding by a peptide element within a tRNA synthetase. Biochemistry, 36, 6739-6744.
    • (1997) Biochemistry , vol.36 , pp. 6739-6744
    • Glasfeld, E.1    Schimmel, P.2
  • 17
    • 0024463581 scopus 로고
    • cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase
    • Jacobo-Molina, A., Peterson, R. and Yang, D.C.H. (1989) cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J. Biol. Chem., 264, 16608-16612.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16608-16612
    • Jacobo-Molina, A.1    Peterson, R.2    Yang, D.C.H.3
  • 18
    • 0028073797 scopus 로고
    • Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII
    • Johnston, M. et al. (1994) Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII. Science, 265, 2077-2082.
    • (1994) Science , vol.265 , pp. 2077-2082
    • Johnston, M.1
  • 19
    • 84889120137 scopus 로고
    • Improved methods for the building of 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. (1991) Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0029959285 scopus 로고    scopus 로고
    • Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A
    • Krovat, B.C. and Jantsch, M.F. (1996) Comparative mutational analysis of the double-stranded RNA binding domains of Xenopus laevis RNA-binding protein A. J. Biol. Chem., 271, 28112-28119.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28112-28119
    • Krovat, B.C.1    Jantsch, M.F.2
  • 21
    • 0024359787 scopus 로고
    • Defining the inside and outside of a catalytic RNA molecule
    • Latham, J.A. and Cech, T.R. (1989) Defining the inside and outside of a catalytic RNA molecule. Science, 245, 276-282.
    • (1989) Science , vol.245 , pp. 276-282
    • Latham, J.A.1    Cech, T.R.2
  • 22
    • 0021099681 scopus 로고
    • Crystallization of a tRNA-aminoacyl-tRNA synthetase complex. Characterization and first crystallographic data
    • Lorber, B., Giegé, R., Ebel, J.-P., Berthet, C. Thierry, J.-C. and Moras, D. (1983) Crystallization of a tRNA-aminoacyl-tRNA synthetase complex. Characterization and first crystallographic data. J. Biol. Chem., 258, 8429-8435.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8429-8435
    • Lorber, B.1    Giegé, R.2    Ebel, J.-P.3    Berthet, C.4    Thierry, J.-C.5    Moras, D.6
  • 23
    • 0023182973 scopus 로고
    • The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase
    • Lorber, B., Kern, D., Mejdoub, H., Boulanger, Y., Reinbolt, J. and Giegé, R. (1987) The microheterogeneity of the crystallizable yeast cytoplasmic aspartyl-tRNA synthetase. Eur. J. Biochem., 165, 409-417.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 409-417
    • Lorber, B.1    Kern, D.2    Mejdoub, H.3    Boulanger, Y.4    Reinbolt, J.5    Giegé, R.6
  • 24
    • 0024289862 scopus 로고
    • Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain
    • Lorber, B., Mejdoub, H., Reinbolt, J., Boulanger, Y. and Giegé, R. (1988) Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain. Eur. J. Biochem., 174, 155-161.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 155-161
    • Lorber, B.1    Mejdoub, H.2    Reinbolt, J.3    Boulanger, Y.4    Giegé, R.5
  • 25
    • 0025847591 scopus 로고
    • A PMR2 tandem repeat with a modified C-terminus is located downstream from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae
    • Martinez, R., Latreille, M.T. and Mirande, M. (1991) A PMR2 tandem repeat with a modified C-terminus is located downstream from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae. Mol. Gen. Genet., 227, 149-154.
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 149-154
    • Martinez, R.1    Latreille, M.T.2    Mirande, M.3
  • 26
    • 0026325311 scopus 로고
    • Interaction of microtubule-associated proteins with microtubules: Yeast lysyl- and valyl-tRNA synthetases and tau 218-235 synthetic peptide as model systems
    • Melki, R., Kerjan, P., Waller, J.-P., Carlier, M.-F. and Pantaloni, D. (1991) Interaction of microtubule-associated proteins with microtubules: yeast lysyl- and valyl-tRNA synthetases and tau 218-235 synthetic peptide as model systems. Biochemistry, 30, 11536-11545.
    • (1991) Biochemistry , vol.30 , pp. 11536-11545
    • Melki, R.1    Kerjan, P.2    Waller, J.-P.3    Carlier, M.-F.4    Pantaloni, D.5
  • 27
    • 0025930249 scopus 로고
    • Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications
    • Mirande, M. (1991) Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucleic Acid Res. Mol. Biol., 40, 95-142.
    • (1991) Prog. Nucleic Acid Res. Mol. Biol. , vol.40 , pp. 95-142
    • Mirande, M.1
  • 28
    • 0024531905 scopus 로고
    • Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase
    • Mirande, M. and Waller, J.-P. (1989) Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase. J. Biol. Chem., 264, 842-847.
    • (1989) J. Biol. Chem. , vol.264 , pp. 842-847
    • Mirande, M.1    Waller, J.-P.2
  • 29
    • 0027361278 scopus 로고
    • Structural aspects and evolutionary implications of the recognition between tRNAs and aminoacyl-tRNA synthetases
    • Moras, D. (1993) Structural aspects and evolutionary implications of the recognition between tRNAs and aminoacyl-tRNA synthetases. Biochimie, 75, 651-657.
    • (1993) Biochimie , vol.75 , pp. 651-657
    • Moras, D.1
  • 30
    • 0025267036 scopus 로고
    • Relaxation of transfer RNA specificity by removal of modified nucleotides
    • Perret, V., Garcia, A., Grosjean, H., Ebel, J.-P., Florentz, C. and Giegé, R. (1990) Relaxation of transfer RNA specificity by removal of modified nucleotides. Nature, 344, 787-789.
    • (1990) Nature , vol.344 , pp. 787-789
    • Perret, V.1    Garcia, A.2    Grosjean, H.3    Ebel, J.-P.4    Florentz, C.5    Giegé, R.6
  • 31
    • 0033534561 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: Identification of protein-protein interactions and characterization of a core protein
    • Quevillon, S., Robinson, J.-C., Berthonneau, E. Siatecka, M. and Mirande, M. (1999) Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J. Mol. Biol., 285, 183-195.
    • (1999) J. Mol. Biol. , vol.285 , pp. 183-195
    • Quevillon, S.1    Robinson, J.-C.2    Berthonneau, E.3    Siatecka, M.4    Mirande, M.5
  • 32
    • 0000282186 scopus 로고    scopus 로고
    • Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex
    • Rho, S.B., Kim, M.J., Lee, J.S., Seol, W., Molegi, 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.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4488-4493
    • Rho, S.B.1    Kim, M.J.2    Lee, J.S.3    Seol, W.4    Molegi, H.5    Kim, S.6    Shiba, K.7
  • 33
    • 0021891233 scopus 로고
    • Asp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetase. A comparative study of the yeast phenylalanine system by phosphate alkylation experiments with ethylnitrosourea
    • Asp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetase. A comparative study of the yeast phenylalanine system by phosphate alkylation experiments with ethylnitrosourea. J. Mol. Biol., 184, 455-471.
    • (1985) J. Mol. Biol. , vol.184 , pp. 455-471
    • Romby, P.1    Moras, D.2    Bergdoll, M.3    Dumas, P.4    Vlassov, V.V.5    Westhof, E.6    Ebel, J.-P.7    Giegé, R.8
  • 34
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost, B. and Sanders, C. (1993) Prediction of protein structure at better than 70% accuracy. J. Mol. Biol., 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sanders, C.2
  • 35
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B. and Sanders, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins, 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sanders, C.2
  • 36
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • Rost, B., Sanders, C. and Schneider, R. (1994) PHD - an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci., 10, 53-60.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sanders, C.2    Schneider, R.3
  • 40
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter, J.M. and Schultz, S.C. (1998) Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J., 17, 7505-7513.
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 41
    • 0032920822 scopus 로고    scopus 로고
    • Crystallogenesis studies on aspartyl-tRNA synthetase: Use of phase diagram to improve crystal quality
    • Sauter, C., Lorber, B., Kern, D., Cavarelli, J., Moras, D. and Giegé, R. (1999) Crystallogenesis studies on aspartyl-tRNA synthetase: use of phase diagram to improve crystal quality. Acta Crystallogr. D, 55, 149-156.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 149-156
    • Sauter, C.1    Lorber, B.2    Kern, D.3    Cavarelli, J.4    Moras, D.5    Giegé, R.6
  • 42
    • 0023061339 scopus 로고
    • Aminoacyl-tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • Schimmel, P. (1987) Aminoacyl-tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu. Rev. Biochem., 56, 125-158.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 43
    • 0032921877 scopus 로고    scopus 로고
    • Getting tRNA synthetases into the nucleus
    • Schimmel, P. and Wang, C.C. (1999) Getting tRNA synthetases into the nucleus. Trends Biochem. Sci., 24, 127-128.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 127-128
    • Schimmel, P.1    Wang, C.C.2
  • 44
    • 0023056460 scopus 로고
    • Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5′ and 3′ termini of AspRS mRNA
    • Sellami, M., Fasiolo, F., Dirheimer, G., Ebel, J.-P. and Gangloff, J. (1986) Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5′ and 3′ termini of AspRS mRNA. Nucleic Acids Res., 14, 1657-1666.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 1657-1666
    • Sellami, M.1    Fasiolo, F.2    Dirheimer, G.3    Ebel, J.-P.4    Gangloff, J.5
  • 45
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc 1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases
    • Simos, G., Segref, A., Fasiolo, F., Hellmuth, K., Shevchenko, A., Mann, M. and Hurt, E.C. (1996) The yeast protein Arc 1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J., 15, 5437-5448.
    • (1996) EMBO J. , vol.15 , pp. 5437-5448
    • Simos, G.1    Segref, A.2    Fasiolo, F.3    Hellmuth, K.4    Shevchenko, A.5    Mann, M.6    Hurt, E.C.7
  • 46
    • 0028238349 scopus 로고
    • Elongation factor Tu: A regulatory GTPase with an integrated effector
    • Sprinzl, M. (1994) Elongation factor Tu: a regulatory GTPase with an integrated effector. Trends Biochem. Sci., 19, 245-250.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 245-250
    • Sprinzl, M.1
  • 47
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. and Higgins, D.G. (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 48
    • 0033523089 scopus 로고    scopus 로고
    • Species barrier to tRNA recognition overcome with nonspecific RNA binding domains
    • Wang, C.-C. and Schimmel, P. (1999) Species barrier to tRNA recognition overcome with nonspecific RNA binding domains. J. Biol. Chem., 274, 16508-16512.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16508-16512
    • Wang, C.-C.1    Schimmel, P.2
  • 49
    • 0000504076 scopus 로고    scopus 로고
    • Rescuing an essential enzyme-RNA complex with a non-essential appended domain
    • Whelihan, E.F. and Schimmel, P. (1997) Rescuing an essential enzyme-RNA complex with a non-essential appended domain. EMBO J., 16, 2968-2974.
    • (1997) EMBO J. , vol.16 , pp. 2968-2974
    • Whelihan, E.F.1    Schimmel, P.2


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