메뉴 건너뛰기




Volumn 18, Issue 6, 2012, Pages 1154-1162

Crystal structure of the Rna14-Rna15 complex

Author keywords

CstF 64; CstF 77; HAT domain; HEAT repeat; Pre mRNA processing; Protein complex

Indexed keywords

CLEAVAGE STIMULATION FACTOR; CLEAVAGE STIMULATION FACTOR 64; CLEAVAGE STIMULATION FACTOR 77; RNA; RNA14; RNA15; UNCLASSIFIED DRUG;

EID: 84861374448     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.032524.112     Document Type: Article
Times cited : (20)

References (27)
  • 1
    • 33947202065 scopus 로고    scopus 로고
    • Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors
    • DOI 10.1016/j.molcel.2007.01.034, PII S1097276507000858
    • Bai Y, Auperin TC, Chou C-Y, Chang G-G, Manley JL, Tong L. 2007a. Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursors. Mol Cell 25: 863-875. (Pubitemid 46436526)
    • (2007) Molecular Cell , vol.25 , Issue.6 , pp. 863-875
    • Bai, Y.1    Auperin, T.C.2    Chou, C.-Y.3    Chang, G.-G.4    Manley, J.L.5    Tong, L.6
  • 4
    • 0030784958 scopus 로고    scopus 로고
    • Mechanism and regulation of mRNA polyadenylation
    • Colgan DF, Manley JL. 1997. Mechanism and regulation of mRNA polyadenylation. Genes Dev 11: 2755-2766. (Pubitemid 27481677)
    • (1997) Genes and Development , vol.11 , Issue.21 , pp. 2755-2766
    • Colgan, D.F.1    Manley, J.L.2
  • 7
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson WA. 1991. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254: 51-58. (Pubitemid 21917315)
    • (1991) Science , vol.254 , Issue.5028 , pp. 51-58
    • Hendrickson, W.A.1
  • 8
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J 9: 1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 10
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building 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
  • 11
    • 34547839747 scopus 로고    scopus 로고
    • The structure of the CstF-77 homodimer provides insights into CstF assembly
    • DOI 10.1093/nar/gkm458
    • Legrand P, Pinaud N, Minvielle-Sebastia L, Fribourg S. 2007. The structure of CstF-77 homodimer provides insights into CstF assembly. Nucleic Acids Res 35: 4515-4522. (Pubitemid 47244602)
    • (2007) Nucleic Acids Research , vol.35 , Issue.13 , pp. 4515-4522
    • Legrand, P.1    Pinaud, N.2    Minvielle-Sebastia, L.3    Fribourg, S.4
  • 13
    • 33845902048 scopus 로고    scopus 로고
    • Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease
    • DOI 10.1038/nature05363, PII NATURE05363
    • Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L. 2006b. Polyadenylation factor CPSF-73 is the premRNA 3′-end-processing endonuclease. Nature 444: 953-956. (Pubitemid 46025011)
    • (2006) Nature , vol.444 , Issue.7121 , pp. 953-956
    • Mandel, C.R.1    Kaneko, S.2    Zhang, H.3    Gebauer, D.4    Vethantham, V.5    Manley, J.L.6    Tong, L.7
  • 14
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3′-end processing
    • Mandel CR, Bai Y, Tong L. 2008. Protein factors in pre-mRNA 3′-end processing. Cell Mol Life Sci 65: 1099-1122.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1099-1122
    • Mandel, C.R.1    Bai, Y.2    Tong, L.3
  • 15
    • 80053190826 scopus 로고    scopus 로고
    • Evidence for a complex of transcription factor IIB (TFIIB) with poly(A) polymerase and cleavage factor I subunits required for gene looping
    • Medler S, Al Husini N, Raghunayakula S, Mukundan B, Aldea A, Ansari A. 2011. Evidence for a complex of transcription factor IIB (TFIIB) with poly(A) polymerase and cleavage factor I subunits required for gene looping. J Biol Chem 286: 33709-33718.
    • (2011) J Biol Chem , vol.286 , pp. 33709-33718
    • Medler, S.1    Al Husini, N.2    Raghunayakula, S.3    Mukundan, B.4    Aldea, A.5    Ansari, A.6
  • 16
    • 0028589505 scopus 로고
    • RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3′-end processing factor
    • Minvielle-Sebastia L, Preker PJ, Keller W. 1994. RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3′-end processing factor. Science 266: 1702-1705.
    • (1994) Science , vol.266 , pp. 1702-1705
    • Minvielle-Sebastia, L.1    Preker, P.J.2    Keller, W.3
  • 17
    • 79953878285 scopus 로고    scopus 로고
    • Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CFIA complex
    • Moreno-Morcillo M, Minvielle-Sebastia L, Fribourg S, Mackereth CD. 2011. Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CFIA complex. Structure 19: 534-545.
    • (2011) Structure , vol.19 , pp. 534-545
    • Moreno-Morcillo, M.1    Minvielle-Sebastia, L.2    Fribourg, S.3    Mackereth, C.D.4
  • 19
    • 3042555841 scopus 로고    scopus 로고
    • Rna14 - Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA
    • DOI 10.1093/nar/gkh664
    • Noble CG, Walker PA, Calder LJ, Taylor IA. 2004. Rna14-Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA. Nucleic Acids Res 32: 3364-3375. (Pubitemid 39117452)
    • (2004) Nucleic Acids Research , vol.32 , Issue.11 , pp. 3364-3375
    • Noble, C.G.1    Walker, P.A.2    Calder, L.J.3    Taylor, I.A.4
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 77953261028 scopus 로고    scopus 로고
    • Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3′-end processing factors
    • Pancevac C, Goldstone DC, Ramos A, Taylor IA. 2010. Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3′-end processing factors. Nucleic Acids Res 38: 3119-3132.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3119-3132
    • Pancevac, C.1    Goldstone, D.C.2    Ramos, A.3    Taylor, I.A.4
  • 22
    • 0031940245 scopus 로고    scopus 로고
    • The HAT helix, a repetitive motif implicated in RNA processing
    • DOI 10.1016/S0968-0004(97)01156-0, PII S0968000497011560
    • Preker PJ, Keller W. 1998. The HAT helix, a repetitive motif implicated in RNA processing. Trends Biochem Sci 23: 15-16. (Pubitemid 28093987)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.1 , pp. 15-16
    • Preker, P.J.1    Keller, W.2
  • 23
    • 33847327963 scopus 로고    scopus 로고
    • The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3′-end processing
    • DOI 10.1074/jbc.M609981200
    • Qu X, Perez-Canadillas JM, Agrawal S, de Baecke J, Cheng H, Varani G, Moore CL. 2007. The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3′-end processing. J Biol Chem 283: 2101-2115. (Pubitemid 47076683)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 2101-2115
    • Qu, X.1    Perez-Canadillas, J.-M.2    Agrawal, S.3    De Baecke, J.4    Cheng, H.5    Varani, G.6    Moore, C.7
  • 24
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated Structure Solution and Density Modification
    • DOI 10.1016/S0076-6879(03)74002-6
    • Terwilliger TC. 2003. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol 374: 22-37. (Pubitemid 37531804)
    • (2003) Methods in Enzymology , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 26
    • 34047252866 scopus 로고    scopus 로고
    • Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis
    • DOI 10.1074/jbc.M610235200
    • Xiang S, Usunow G, Lange G, Busch M, Tong L. 2007. Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis. J Biol Chem 282: 2676-2682. (Pubitemid 47076757)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2676-2682
    • Xiang, S.1    Usunow, G.2    Lange, G.3    Busch, M.4    Tong, L.5
  • 27
    • 0033059981 scopus 로고    scopus 로고
    • Formation of mRNA 3' ends in eukaryotes: Mechanism, regulation, and interrelationships with other steps in mRNA synthesis
    • Zhao J, Hyman L, Moore CL. 1999. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol Mol Biol Rev 63: 405-445. (Pubitemid 29264977)
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.2 , pp. 405-445
    • Zhao, J.1    Hyman, L.2    Moore, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.