메뉴 건너뛰기




Volumn 25, Issue 3, 2007, Pages 399-411

The 5′ End of U2 snRNA Is in Close Proximity to U1 and Functional Sites of the Pre-mRNA in Early Spliceosomal Complexes

Author keywords

CELLCYCLE

Indexed keywords

EDETIC ACID; HYDROXYL RADICAL; IRON; IRON 1 (4 BROMOACETOMIDOBENZYL)EDETIC ACID; MESSENGER RNA PRECURSOR; SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; UNCLASSIFIED DRUG; 1 (4 BROMOACETAMIDOBENZYL)EDTA; 1-(4-BROMOACETAMIDOBENZYL)EDTA; DRUG DERIVATIVE; MESSENGER RNA; RNA PRECURSOR; U1 SMALL NUCLEAR RNA; U2 SMALL NUCLEAR RNA;

EID: 33846665912     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.12.019     Document Type: Article
Times cited : (42)

References (48)
  • 1
    • 0030911051 scopus 로고    scopus 로고
    • Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals
    • Abovich N., and Rosbash M. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell 89 (1997) 403-412
    • (1997) Cell , vol.89 , pp. 403-412
    • Abovich, N.1    Rosbash, M.2
  • 2
    • 0037279013 scopus 로고    scopus 로고
    • Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding
    • Banerjee H., Rahn A., Davis W., and Singh R. Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding. RNA 9 (2003) 88-99
    • (2003) RNA , vol.9 , pp. 88-99
    • Banerjee, H.1    Rahn, A.2    Davis, W.3    Singh, R.4
  • 3
    • 0026661948 scopus 로고
    • Protein components specifically associated with prespliceosome and spliceosome complexes
    • Bennett M., Michaud S., Kingston J., and Reed R. Protein components specifically associated with prespliceosome and spliceosome complexes. Genes Dev. 6 (1992) 1986-2000
    • (1992) Genes Dev. , vol.6 , pp. 1986-2000
    • Bennett, M.1    Michaud, S.2    Kingston, J.3    Reed, R.4
  • 4
    • 3142675143 scopus 로고    scopus 로고
    • Ser/Arg-rich protein-mediated communication between U1 and U2 small nuclear ribonucleoprotein particles
    • Boukis L.A., Liu N., Furuyama S., and Bruzik J.P. Ser/Arg-rich protein-mediated communication between U1 and U2 small nuclear ribonucleoprotein particles. J. Biol. Chem. 279 (2004) 29647-29653
    • (2004) J. Biol. Chem. , vol.279 , pp. 29647-29653
    • Boukis, L.A.1    Liu, N.2    Furuyama, S.3    Bruzik, J.P.4
  • 5
    • 0029118221 scopus 로고
    • Accumulation of a novel spliceosomal complex on pre-mRNAs containing branch site mutations
    • Champion-Arnaud P., Gozani O., Palandjian L., and Reed R. Accumulation of a novel spliceosomal complex on pre-mRNAs containing branch site mutations. Mol. Cell. Biol. 15 (1995) 5750-5756
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5750-5756
    • Champion-Arnaud, P.1    Gozani, O.2    Palandjian, L.3    Reed, R.4
  • 6
    • 0029894931 scopus 로고    scopus 로고
    • Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly
    • Chiara M.D., Gozani O., Bennett M., Champion-Arnaud P., Palandjian L., and Reed R. Identification of proteins that interact with exon sequences, splice sites, and the branchpoint sequence during each stage of spliceosome assembly. Mol. Cell. Biol. 16 (1996) 3317-3326
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3317-3326
    • Chiara, M.D.1    Gozani, O.2    Bennett, M.3    Champion-Arnaud, P.4    Palandjian, L.5    Reed, R.6
  • 7
    • 0030750730 scopus 로고    scopus 로고
    • Evidence that U5 snRNP recognizes the 3′ splice site for catalytic step II in mammals
    • Chiara M.D., Palandjian L., Feld Kramer R., and Reed R. Evidence that U5 snRNP recognizes the 3′ splice site for catalytic step II in mammals. EMBO J. 16 (1997) 4746-4759
    • (1997) EMBO J. , vol.16 , pp. 4746-4759
    • Chiara, M.D.1    Palandjian, L.2    Feld Kramer, R.3    Reed, R.4
  • 8
    • 0033655152 scopus 로고    scopus 로고
    • Directed hydroxyl radical probing of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes
    • Culver G.M., and Noller H.F. Directed hydroxyl radical probing of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes. Methods Enzymol. 318 (2000) 461-475
    • (2000) Methods Enzymol. , vol.318 , pp. 461-475
    • Culver, G.M.1    Noller, H.F.2
  • 9
    • 0032880119 scopus 로고    scopus 로고
    • Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155
    • Das B.K., Xia L., Palandjian L., Gozani O., Chyung Y., and Reed R. Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol. Cell. Biol. 19 (1999) 6796-6802
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6796-6802
    • Das, B.K.1    Xia, L.2    Palandjian, L.3    Gozani, O.4    Chyung, Y.5    Reed, R.6
  • 10
    • 0033636518 scopus 로고    scopus 로고
    • Functional association of U2 snRNP with the ATP-independent spliceosomal complex E
    • Das R., Zhou Z., and Reed R. Functional association of U2 snRNP with the ATP-independent spliceosomal complex E. Mol. Cell 5 (2000) 779-787
    • (2000) Mol. Cell , vol.5 , pp. 779-787
    • Das, R.1    Zhou, Z.2    Reed, R.3
  • 11
    • 33745860086 scopus 로고    scopus 로고
    • Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions
    • Deckert J., Hartmuth K., Boehringer D., Behzadnia N., Will C.L., Kastner B., Stark H., Urlaub H., and Lührmann R. Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions. Mol. Cell. Biol. 26 (2006) 5528-5543
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5528-5543
    • Deckert, J.1    Hartmuth, K.2    Boehringer, D.3    Behzadnia, N.4    Will, C.L.5    Kastner, B.6    Stark, H.7    Urlaub, H.8    Lührmann, R.9
  • 12
    • 0019883215 scopus 로고
    • Synthesis of mono- and dinucleotide photoaffinity probes of ribonucleic acid polymerase
    • DeRiemer L.H., and Meares C.F. Synthesis of mono- and dinucleotide photoaffinity probes of ribonucleic acid polymerase. Biochemistry 20 (1981) 1606-1612
    • (1981) Biochemistry , vol.20 , pp. 1606-1612
    • DeRiemer, L.H.1    Meares, C.F.2
  • 13
    • 9344271506 scopus 로고    scopus 로고
    • Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomal E-complex formation
    • Dönmez G., Hartmuth K., and Lührmann R. Modified nucleotides at the 5′ end of human U2 snRNA are required for spliceosomal E-complex formation. RNA 10 (2004) 1925-1933
    • (2004) RNA , vol.10 , pp. 1925-1933
    • Dönmez, G.1    Hartmuth, K.2    Lührmann, R.3
  • 14
    • 0029562737 scopus 로고
    • The global folding of four-way helical junctions in RNA, including that in U1 snRNA
    • Duckett D.R., Murchie A.I., and Lilley D.M. The global folding of four-way helical junctions in RNA, including that in U1 snRNA. Cell 83 (1995) 1027-1036
    • (1995) Cell , vol.83 , pp. 1027-1036
    • Duckett, D.R.1    Murchie, A.I.2    Lilley, D.M.3
  • 15
    • 33645212088 scopus 로고    scopus 로고
    • U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes
    • Dybkov O., Will C.L., Deckert J., Behzadnia N., Hartmuth K., and Lührmann R. U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes. Mol. Cell. Biol. 26 (2006) 2803-2816
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2803-2816
    • Dybkov, O.1    Will, C.L.2    Deckert, J.3    Behzadnia, N.4    Hartmuth, K.5    Lührmann, R.6
  • 16
    • 0033119176 scopus 로고    scopus 로고
    • Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions
    • Frilander M.J., and Steitz J.A. Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions. Genes Dev. 13 (1999) 851-863
    • (1999) Genes Dev. , vol.13 , pp. 851-863
    • Frilander, M.J.1    Steitz, J.A.2
  • 17
    • 20344369784 scopus 로고    scopus 로고
    • Proximity of the U12 snRNA with both the 5′ splice site and the branch point during early stages of spliceosome assembly
    • Frilander M.J., and Meng X. Proximity of the U12 snRNA with both the 5′ splice site and the branch point during early stages of spliceosome assembly. Mol. Cell. Biol. 25 (2005) 4813-4825
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4813-4825
    • Frilander, M.J.1    Meng, X.2
  • 18
    • 0026599345 scopus 로고
    • The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3′ splice site
    • Fu X.D., and Maniatis T. The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3′ splice site. Proc. Natl. Acad. Sci. USA 89 (1992) 1725-1729
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1725-1729
    • Fu, X.D.1    Maniatis, T.2
  • 19
    • 0030044836 scopus 로고    scopus 로고
    • Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A
    • Gozani O., Feld R., and Reed R. Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A. Genes Dev. 10 (1996) 233-243
    • (1996) Genes Dev. , vol.10 , pp. 233-243
    • Gozani, O.1    Feld, R.2    Reed, R.3
  • 20
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site
    • Gozani O., Potashkin J., and Reed R. A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. Mol. Cell. Biol. 18 (1998) 4752-4760
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 21
    • 0028360967 scopus 로고
    • Visualization of RNA tertiary structure by RNA-EDTA.Fe(II) autocleavage: analysis of tRNA(Phe) with uridine-EDTA.Fe(II) at position 47
    • Han H., and Dervan P.B. Visualization of RNA tertiary structure by RNA-EDTA.Fe(II) autocleavage: analysis of tRNA(Phe) with uridine-EDTA.Fe(II) at position 47. Proc. Natl. Acad. Sci. USA 91 (1994) 4955-4959
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4955-4959
    • Han, H.1    Dervan, P.B.2
  • 22
    • 0033534531 scopus 로고    scopus 로고
    • An unusual chemical reactivity of Sm site adenosines strongly correlates with proper assembly of core U snRNP particles
    • Hartmuth K., Raker V.A., Huber J., Branlant C., and Lührmann R. An unusual chemical reactivity of Sm site adenosines strongly correlates with proper assembly of core U snRNP particles. J. Mol. Biol. 285 (1999) 133-147
    • (1999) J. Mol. Biol. , vol.285 , pp. 133-147
    • Hartmuth, K.1    Raker, V.A.2    Huber, J.3    Branlant, C.4    Lührmann, R.5
  • 23
    • 0033655139 scopus 로고    scopus 로고
    • Directed hydroxyl radical probing using iron(II) tethered to RNA
    • Joseph S., and Noller H.F. Directed hydroxyl radical probing using iron(II) tethered to RNA. Methods Enzymol. 318 (2000) 175-190
    • (2000) Methods Enzymol. , vol.318 , pp. 175-190
    • Joseph, S.1    Noller, H.F.2
  • 24
    • 0033962573 scopus 로고    scopus 로고
    • Calculation of the relative geometry of tRNAs in the ribosome from directed hydroxyl-radical probing data
    • Joseph S., Whirl M.L., Kondo D., Noller H.F., and Altman R.B. Calculation of the relative geometry of tRNAs in the ribosome from directed hydroxyl-radical probing data. RNA 6 (2000) 220-232
    • (2000) RNA , vol.6 , pp. 220-232
    • Joseph, S.1    Whirl, M.L.2    Kondo, D.3    Noller, H.F.4    Altman, R.B.5
  • 25
    • 0030027483 scopus 로고    scopus 로고
    • Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle
    • Kao H.Y., and Siliciano P.G. Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle. Mol. Cell. Biol. 16 (1996) 960-967
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 960-967
    • Kao, H.Y.1    Siliciano, P.G.2
  • 26
    • 0026596044 scopus 로고
    • Structure of the small nuclear RNP particle U1: identification of the two structural protuberances with RNP-antigens A and 70K
    • Kastner B., Kornstadt U., Bach M., and Lührmann R. Structure of the small nuclear RNP particle U1: identification of the two structural protuberances with RNP-antigens A and 70K. J. Cell Biol. 116 (1992) 839-849
    • (1992) J. Cell Biol. , vol.116 , pp. 839-849
    • Kastner, B.1    Kornstadt, U.2    Bach, M.3    Lührmann, R.4
  • 27
    • 0036315512 scopus 로고    scopus 로고
    • Early organization of pre-mRNA during spliceosome assembly
    • Kent O.A., and MacMillan A.M. Early organization of pre-mRNA during spliceosome assembly. Nat. Struct. Biol. 9 (2002) 576-581
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 576-581
    • Kent, O.A.1    MacMillan, A.M.2
  • 29
    • 0025340544 scopus 로고
    • Solution structure of human U1 snRNA. Derivation of a possible three- dimensional model
    • Krol A., Westhof E., Bach M., Lührmann R., Ebel J.P., and Carbon P. Solution structure of human U1 snRNA. Derivation of a possible three- dimensional model. Nucleic Acids Res. 18 (1990) 3803-3811
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3803-3811
    • Krol, A.1    Westhof, E.2    Bach, M.3    Lührmann, R.4    Ebel, J.P.5    Carbon, P.6
  • 30
    • 0029737855 scopus 로고    scopus 로고
    • A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5′ splice site
    • Lewis J.D., Izaurralde E., Jarmolowski A., McGuigan C., and Mattaj I.W. A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5′ splice site. Genes Dev. 10 (1996) 1683-1698
    • (1996) Genes Dev. , vol.10 , pp. 1683-1698
    • Lewis, J.D.1    Izaurralde, E.2    Jarmolowski, A.3    McGuigan, C.4    Mattaj, I.W.5
  • 32
    • 0027215924 scopus 로고
    • A functional association between the 5′ and 3′ splice site is established in the earliest prespliceosome complex (E) in mammals
    • Michaud S., and Reed R. A functional association between the 5′ and 3′ splice site is established in the earliest prespliceosome complex (E) in mammals. Genes Dev. 7 (1993) 1008-1020
    • (1993) Genes Dev. , vol.7 , pp. 1008-1020
    • Michaud, S.1    Reed, R.2
  • 33
    • 0032993062 scopus 로고    scopus 로고
    • Directed hydroxyl radical probing of 16S rRNA in the ribosome: spatial proximity of RNA elements of the 3′ and 5′ domains
    • Newcomb L.F., and Noller H.F. Directed hydroxyl radical probing of 16S rRNA in the ribosome: spatial proximity of RNA elements of the 3′ and 5′ domains. RNA 5 (1999) 849-855
    • (1999) RNA , vol.5 , pp. 849-855
    • Newcomb, L.F.1    Noller, H.F.2
  • 34
    • 0036161499 scopus 로고    scopus 로고
    • The spliceosome: no assembly required?
    • Nilsen T.W. The spliceosome: no assembly required?. Mol. Cell 9 (2002) 8-9
    • (2002) Mol. Cell , vol.9 , pp. 8-9
    • Nilsen, T.W.1
  • 35
    • 0345169036 scopus 로고    scopus 로고
    • Splicing double: insights from the second spliceosome
    • Patel A.A., and Steitz J.A. Splicing double: insights from the second spliceosome. Nat. Rev. Mol. Cell Biol. 4 (2003) 960-970
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 960-970
    • Patel, A.A.1    Steitz, J.A.2
  • 36
    • 0029917043 scopus 로고    scopus 로고
    • Three recognition events at the branch-site adenine
    • Query C.C., Strobel S.A., and Sharp P.A. Three recognition events at the branch-site adenine. EMBO J. 15 (1996) 1392-1402
    • (1996) EMBO J. , vol.15 , pp. 1392-1402
    • Query, C.C.1    Strobel, S.A.2    Sharp, P.A.3
  • 37
    • 0034069505 scopus 로고    scopus 로고
    • Mechanisms of fidelity in pre-mRNA splicing
    • Reed R. Mechanisms of fidelity in pre-mRNA splicing. Curr. Opin. Cell Biol. 12 (2000) 340-345
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 340-345
    • Reed, R.1
  • 38
    • 33745755054 scopus 로고    scopus 로고
    • Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes
    • Rhode B.M., Hartmuth K., Westhof E., and Lührmann R. Proximity of conserved U6 and U2 snRNA elements to the 5′ splice site region in activated spliceosomes. EMBO J. 25 (2006) 2475-2486
    • (2006) EMBO J. , vol.25 , pp. 2475-2486
    • Rhode, B.M.1    Hartmuth, K.2    Westhof, E.3    Lührmann, R.4
  • 39
    • 0034098296 scopus 로고    scopus 로고
    • Differential recognition of the polypyrimidine-tract by the general splicing factor U2AF65 and the splicing repressor sex-lethal
    • Singh R., Banerjee H., and Green M.R. Differential recognition of the polypyrimidine-tract by the general splicing factor U2AF65 and the splicing repressor sex-lethal. RNA 6 (2000) 901-911
    • (2000) RNA , vol.6 , pp. 901-911
    • Singh, R.1    Banerjee, H.2    Green, M.R.3
  • 40
    • 0028006713 scopus 로고
    • SR proteins promote the first specific recognition of pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex
    • Staknis D., and Reed R. SR proteins promote the first specific recognition of pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex. Mol. Cell. Biol. 14 (1994) 7670-7682
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7670-7682
    • Staknis, D.1    Reed, R.2
  • 41
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley J.P., and Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92 (1998) 315-326
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 42
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    • Stark H., Dube P., Lührmann R., and Kastner B. Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle. Nature 409 (2001) 539-542
    • (2001) Nature , vol.409 , pp. 539-542
    • Stark, H.1    Dube, P.2    Lührmann, R.3    Kastner, B.4
  • 43
    • 0026517751 scopus 로고
    • Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme
    • Wang J.F., and Cech T.R. Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme. Science 256 (1992) 526-529
    • (1992) Science , vol.256 , pp. 526-529
    • Wang, J.F.1    Cech, T.R.2
  • 44
    • 0026561544 scopus 로고
    • The low-abundance U11 and U12 small nuclear ribonucleoproteins (snRNPs) interact to form a two-snRNP complex
    • Wassarman K.M., and Steitz J.A. The low-abundance U11 and U12 small nuclear ribonucleoproteins (snRNPs) interact to form a two-snRNP complex. Mol. Cell. Biol. 12 (1992) 1276-1285
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1276-1285
    • Wassarman, K.M.1    Steitz, J.A.2
  • 46
    • 1542380571 scopus 로고    scopus 로고
    • Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA
    • Xu Y.Z., Newnham C.M., Kameoka S., Huang T., Konarska M.M., and Query C.C. Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA. EMBO J. 23 (2004) 376-385
    • (2004) EMBO J. , vol.23 , pp. 376-385
    • Xu, Y.Z.1    Newnham, C.M.2    Kameoka, S.3    Huang, T.4    Konarska, M.M.5    Query, C.C.6
  • 47
    • 0026569967 scopus 로고
    • Cloning and domain structure of the mammalian splicing factor U2AF
    • Zamore P.D., Patton J.G., and Green M.R. Cloning and domain structure of the mammalian splicing factor U2AF. Nature 355 (1992) 609-614
    • (1992) Nature , vol.355 , pp. 609-614
    • Zamore, P.D.1    Patton, J.G.2    Green, M.R.3
  • 48
    • 0023845346 scopus 로고
    • Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles
    • Zillmann M., Zapp M.L., and Berget S.M. Gel electrophoretic isolation of splicing complexes containing U1 small nuclear ribonucleoprotein particles. Mol. Cell. Biol. 8 (1988) 814-821
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 814-821
    • Zillmann, M.1    Zapp, M.L.2    Berget, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.