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Volumn 50, Issue 47, 2011, Pages 10203-10214

Reconstitution of CF IA from Overexpressed subunits reveals stoichiometry and provides insights into molecular topology

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL METHODS; CATALYTIC SUBUNITS; DIMER INTERFACE; MOLECULAR TOPOLOGIES; POLYADENYLATION; PROTEIN COMPLEXES; SIGNAL SEQUENCE; STRUCTURAL ORGANIZATION; TOPOLOGICAL MODELS;

EID: 81855190895     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200964p     Document Type: Article
Times cited : (25)

References (47)
  • 1
    • 77953284100 scopus 로고    scopus 로고
    • Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation
    • Millevoi, S. and Vagner, S. (2010) Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation Nucleic Acids Res. 38, 2757-2774
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2757-2774
    • Millevoi, S.1    Vagner, S.2
  • 2
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3′-end processing
    • Mandel, C. R., Bai, Y., and 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
  • 3
    • 38949111543 scopus 로고    scopus 로고
    • 3′ end mRNA processing: Molecular mechanisms and implications for health and disease
    • DOI 10.1038/sj.emboj.7601932, PII 7601932
    • Danckwardt, S., Hentze, M. W., and Kulozik, A. E. (2008) 3′ end mRNA processing: molecular mechanisms and implications for health and disease EMBO J. 27, 482-498 (Pubitemid 351225676)
    • (2008) EMBO Journal , vol.27 , Issue.3 , pp. 482-498
    • Danckwardt, S.1    Hentze, M.W.2    Kulozik, A.E.3
  • 4
    • 0034602833 scopus 로고    scopus 로고
    • The WD-repeat protein Pfs2p bridges two essential factors within the yeast pre-mRNA 3'-end-processing complex
    • Ohnacker, M., Barabino, S. M., Preker, P. J., and Keller, W. (2000) The WD-repeat protein pfs2p bridges two essential factors within the yeast pre-mRNA 3′-end-processing complex EMBO J. 19, 37-47 (Pubitemid 30009223)
    • (2000) EMBO Journal , vol.19 , Issue.1 , pp. 37-47
    • Ohnacker, M.1    Barabino, S.M.L.2    Preker, P.J.3    Keller, W.4
  • 5
    • 0026656539 scopus 로고
    • Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA
    • Chen, J. and Moore, C. (1992) Separation of factors required for cleavage and polyadenylation of yeast pre-mRNA Mol. Cell. Biol. 12, 3470-3481
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3470-3481
    • Chen, J.1    Moore, C.2
  • 6
    • 0029910068 scopus 로고    scopus 로고
    • Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3' ends
    • DOI 10.1074/jbc.271.43.27167
    • Kessler, M. M., Zhao, J., and Moore, C. L. (1996) Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3′ ends J. Biol. Chem. 271, 27167-27175 (Pubitemid 26359139)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 27167-27175
    • Kessler, M.M.1    Zhao, J.2    Moore, C.L.3
  • 7
    • 33845902048 scopus 로고    scopus 로고
    • Polyadenylation factor CPSF-73 is the pre-mRNA 3′-end-processing endonuclease
    • DOI 10.1038/nature05363, PII NATURE05363
    • Mandel, C. R., Kaneko, S., Zhang, H., Gebauer, D., Vethantham, V., Manley, J. L., and Tong, L. (2006) Polyadenylation factor CPSF-73 is the pre-mRNA 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
  • 8
    • 34548382114 scopus 로고    scopus 로고
    • Mechanism of Poly(A) Polymerase: Structure of the Enzyme-MgATP-RNA Ternary Complex and Kinetic Analysis
    • DOI 10.1016/j.str.2007.07.010, PII S0969212607002833
    • Balbo, P. B. and Bohm, A. (2007) Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis Structure 15, 1117-1131 (Pubitemid 47362691)
    • (2007) Structure , vol.15 , Issue.9 , pp. 1117-1131
    • Balbo, P.B.1    Bohm, A.2
  • 11
    • 0034544815 scopus 로고    scopus 로고
    • Pre-mRNA processing factors are required for nuclear export
    • DOI 10.1017/S1355838200001059
    • Brodsky, A. S. and Silver, P. A. (2000) Pre-mRNA processing factors are required for nuclear export RNA 6, 1737-1749 (Pubitemid 32001945)
    • (2000) RNA , vol.6 , Issue.12 , pp. 1737-1749
    • Brodsky, A.S.1    Silver, P.A.2
  • 13
    • 77949538391 scopus 로고    scopus 로고
    • Reprogramming of 3′ untranslated regions of mRNAs by alternative polyadenylation in generation of pluripotent stem cells from different cell types
    • Ji, Z. and Tian, B. (2009) Reprogramming of 3′ untranslated regions of mRNAs by alternative polyadenylation in generation of pluripotent stem cells from different cell types PLoS One 4, e8419
    • (2009) PLoS One , vol.4 , pp. 8419
    • Ji, Z.1    Tian, B.2
  • 14
    • 79953014914 scopus 로고    scopus 로고
    • Complex and dynamic landscape of RNA polyadenylation revealed by PAS-Seq
    • Shepard, P. J., Choi, E.-A., Lu, J., Flanagan, L. A., Hertel, K. J., and Shi, Y. (2011) Complex and dynamic landscape of RNA polyadenylation revealed by PAS-Seq RNA 17, 761-772
    • (2011) RNA , vol.17 , pp. 761-772
    • Shepard, P.J.1    Choi, E.-A.2    Lu, J.3    Flanagan, L.A.4    Hertel, K.J.5    Shi, Y.6
  • 15
    • 15544384891 scopus 로고    scopus 로고
    • Computational analysis of 3′-ends of ESTs shows four classes of alternative polyadenylation in human, mouse, and rat
    • DOI 10.1101/gr.3109605
    • Yan, J. and Marr, T. G. (2005) Computational analysis of 3′-ends of ESTs shows four classes of alternative polyadenylation in human, mouse, and rat Genome Res. 15, 369-375 (Pubitemid 40467778)
    • (2005) Genome Research , vol.15 , Issue.3 , pp. 369-375
    • Yan, J.1    Marr, T.G.2
  • 16
    • 13744254695 scopus 로고    scopus 로고
    • A large-scale analysis of mRNA polyadenylation of human and mouse genes
    • DOI 10.1093/nar/gki158
    • Tian, B., Hu, J., Zhang, H., and Lutz, C. S. (2005) A large-scale analysis of mRNA polyadenylation of human and mouse genes Nucleic Acids Res. 33, 201-212 (Pubitemid 40276942)
    • (2005) Nucleic Acids Research , vol.33 , Issue.1 , pp. 201-212
    • Tian, B.1    Hu, J.2    Zhang, H.3    Lutz, C.S.4
  • 17
    • 78650972252 scopus 로고    scopus 로고
    • 201AD) Formation, regulation and evolution of Caenorhabditis elegans 3′UTRs
    • (
    • Jan, C. H., Friedman, R. C., Ruby, J. G., and Bartel, D. P. (201AD) Formation, regulation and evolution of Caenorhabditis elegans 3′UTRs, Nature 469, 97-101.
    • Nature , vol.469 , pp. 97-101
    • Jan, C.H.1    Friedman, R.C.2    Ruby, J.G.3    Bartel, D.P.4
  • 18
    • 55449121696 scopus 로고    scopus 로고
    • Revealing posttranscriptional regulatory elements through network-level conservation
    • Chan, C. S., Elemento, O., and Tavazoie, S. (2005) Revealing posttranscriptional regulatory elements through network-level conservation PLoS Comput. Biol 1, e69
    • (2005) PLoS Comput. Biol , vol.1 , pp. 69
    • Chan, C.S.1    Elemento, O.2    Tavazoie, S.3
  • 19
    • 60149095444 scopus 로고    scopus 로고
    • Most mammalian mRNAs are conserved targets of microRNAs
    • Friedman, R. C., Farh, K. K.-H., Burge, C. B., and Bartel, D. P. (2009) Most mammalian mRNAs are conserved targets of microRNAs Genome Res. 19, 92-105
    • (2009) Genome Res. , vol.19 , pp. 92-105
    • Friedman, R.C.1    Farh, K.K.-H.2    Burge, C.B.3    Bartel, D.P.4
  • 20
    • 53249143880 scopus 로고    scopus 로고
    • 3′ UTRs are the primary regulators of gene expression in the C. elegans germline
    • Merritt, C., Rasoloson, D., Ko, D., and Seydoux, G. (2008) 3′ UTRs are the primary regulators of gene expression in the C. elegans germline Curr. Biol. 18, 1476-1482
    • (2008) Curr. Biol. , vol.18 , pp. 1476-1482
    • Merritt, C.1    Rasoloson, D.2    Ko, D.3    Seydoux, G.4
  • 21
    • 46249092601 scopus 로고    scopus 로고
    • Proliferating cells express mRNAs with shortened 3′ untranslated regions and fewer microRNA target sites
    • DOI 10.1126/science.1155390
    • Sandberg, R., Neilson, J. R., Sarma, A., and Sharp, P. A. (2008) Proliferating cells express mRNAs with shortened 3′ untranslated regions and fewer microRNA target sites Science 320, 1643-1647 (Pubitemid 351931255)
    • (2008) Science , vol.320 , Issue.5883 , pp. 1643-1647
    • Sandberg, R.1    Neilson, J.R.2    Sarma, A.3    Sharp, P.A.4    Burge, C.B.5
  • 22
    • 68749113985 scopus 로고    scopus 로고
    • Widespread shortening of 3′UTRs by alternative cleavage and polyadenylation activates oncogenes in cancer cells
    • Mayr, C. and Bartel, D. P. (2009) Widespread shortening of 3′UTRs by alternative cleavage and polyadenylation activates oncogenes in cancer cells Cell 138, 673-684
    • (2009) Cell , vol.138 , pp. 673-684
    • Mayr, C.1    Bartel, D.P.2
  • 23
    • 79955554179 scopus 로고    scopus 로고
    • Differential genome-wide profiling of tandem 3′ UTRs among human breast cancer and normal cells by high-throughput sequencing
    • Fu, Y., Sun, Y., Li, Y., Li, J., Rao, X., Chen, C., and Xu, A. (2011) Differential genome-wide profiling of tandem 3′ UTRs among human breast cancer and normal cells by high-throughput sequencing Genome Res. 21, 741-747
    • (2011) Genome Res. , vol.21 , pp. 741-747
    • Fu, Y.1    Sun, Y.2    Li, Y.3    Li, J.4    Rao, X.5    Chen, C.6    Xu, A.7
  • 24
    • 0035933149 scopus 로고    scopus 로고
    • Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I
    • DOI 10.1073/pnas.101046598
    • Gross, S. and Moore, C. (2001) Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I Proc. Natl. Acad. Sci. U. S. A. 98, 6080-6085 (Pubitemid 32488196)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.11 , pp. 6080-6085
    • Gross, S.1    Moore, C.2
  • 25
    • 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, C. G., Walker, P. A., Calder, L. J., and Taylor, I. A. (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
  • 26
    • 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, T. C., Chou, C.-Y., Chang, G.-G., Manley, J. L., and Tong, L. (2007) 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
  • 27
    • 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-Sébastia, L., and Fribourg, S. (2007) The structure of the 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
  • 28
    • 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, J.-M., Agrawal, S., De Baecke, J., Cheng, H., Varani, G., and Moore, C. (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. 282, 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
  • 29
    • 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, D. C., Ramos, A., and Taylor, I. A. (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
  • 30
    • 0037507248 scopus 로고    scopus 로고
    • Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein
    • DOI 10.1093/emboj/cdg259
    • Pérez Can̂adillas, J. M. and Varani, G. (2003) Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein EMBO J. 22, 2821-2830 (Pubitemid 36712377)
    • (2003) EMBO Journal , vol.22 , Issue.11 , pp. 2821-2830
    • Perez Canadillas, J.M.1    Varani, G.2
  • 31
    • 3142615882 scopus 로고    scopus 로고
    • Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors
    • DOI 10.1038/nature02679
    • Meinhart, A. and Cramer, P. (2004) Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors Nature 430, 223-226 (Pubitemid 38902432)
    • (2004) Nature , vol.430 , Issue.6996 , pp. 223-226
    • Meinhart, A.1    Cramer, P.2
  • 32
    • 33846688769 scopus 로고    scopus 로고
    • Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor
    • DOI 10.1093/nar/gkl1010
    • Noble, C. G., Beuth, B., and Taylor, I. A. (2007) Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor Nucleic Acids Res. 35, 87-99 (Pubitemid 46189834)
    • (2007) Nucleic Acids Research , vol.35 , Issue.1 , pp. 87-99
    • Noble, C.G.1    Beuth, B.2    Taylor, I.A.3
  • 33
    • 33746296753 scopus 로고    scopus 로고
    • Grabbing the message: Structural basis of mRNA 3′UTR recognition by Hrp1
    • DOI 10.1038/sj.emboj.7601190, PII 7601190
    • Pérez-Can̂adillas, J. M. (2006) Grabbing the message: structural basis of mRNA 3′UTR recognition by Hrp1 EMBO J. 25, 3167-3178 (Pubitemid 44106767)
    • (2006) EMBO Journal , vol.25 , Issue.13 , pp. 3167-3178
    • Perez-Caadillas, J.M.1
  • 34
    • 77955273066 scopus 로고    scopus 로고
    • Novel Protein-Protein Contacts Facilitate mRNA 3′-Processing Signal Recognition by Rna15 and Hrp1
    • Leeper, T. C., Qu, X., Lu, C., Moore, C., and Varani, G. (2010) Novel Protein-Protein Contacts Facilitate mRNA 3′-Processing Signal Recognition by Rna15 and Hrp1 J. Mol. Biol. 401, 334-349
    • (2010) J. Mol. Biol. , vol.401 , pp. 334-349
    • Leeper, T.C.1    Qu, X.2    Lu, C.3    Moore, C.4    Varani, G.5
  • 35
    • 79953878285 scopus 로고    scopus 로고
    • Locked Tether Formation by Cooperative Folding of Rna14p Monkeytail and Rna15p Hinge Domains in the Yeast CF IA Complex
    • Moreno-Morcillo, M., Minvielle-Sébastia, L., Fribourg, S., and Mackereth, C. D. (2011) Locked Tether Formation by Cooperative Folding of Rna14p Monkeytail and Rna15p Hinge Domains in the Yeast CF IA Complex Structure 19, 534-545
    • (2011) Structure , vol.19 , pp. 534-545
    • Moreno-Morcillo, M.1    Minvielle-Sébastia, L.2    Fribourg, S.3    MacKereth, C.D.4
  • 36
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., Trueheart, J., Natsoulis, G., and Fink, G. R. (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genetics Methods Enzymol. 154, 164-175
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 37
    • 0028316883 scopus 로고
    • Cellular localization of RNA14p and RNA15p, two yeast proteins involved in mRNA stability
    • Bonneaud, N., Minvielle-Sebastia, L., Cullin, C., and Lacroute, F. (1994) Cellular localization of RNA14p and RNA15p, two yeast proteins involved in mRNA stability J. Cell. Sci 107 (Pt 4) 913-921 (Pubitemid 24119350)
    • (1994) Journal of Cell Science , vol.107 , Issue.4 , pp. 913-921
    • Bonneaud, N.1    Minvielle-Sebastia, L.2    Cullin, C.3    Lacroute, F.4
  • 38
    • 0032721092 scopus 로고    scopus 로고
    • Pta1, a component of yeast CF II, is required for both cleavage and Poly(A) addition of mRNA precursor
    • Zhao, J., Kessler, M. M., Helmling, S., O'Connor, J. P., and Moore, C. L. (1999) Pta1,a component of yeast CF II, is required for both cleavage and poly(A) addition of mRNA precursor Mol. Cell. Biol. 19 (11) 7733-40 (Pubitemid 29493437)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.11 , pp. 7733-7740
    • Zhao, J.1    Kessler, M.2    Helmling, S.3    O'Connor, J.P.4    Moore, C.5
  • 39
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • DOI 10.1016/j.bpc.2003.10.028, PII S0301462203003090
    • Stafford, W. F. and Sherwood, P. J. (2004) Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants Biophys. Chem. 108, 231-243 (Pubitemid 38388491)
    • (2004) Biophysical Chemistry , vol.108 , Issue.1-3 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 40
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25, 495-503 (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 42
    • 1642546383 scopus 로고    scopus 로고
    • Computation and Analysis of Protein Circular Dichroism Spectra
    • DOI 10.1016/S0076-6879(04)83013-1
    • Sreerama, N. and Woody, R. W. (2004) Computation and analysis of protein circular dichroism spectra Methods Enzymol. 383, 318-351 (Pubitemid 38401795)
    • (2004) Methods in Enzymology , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 43
    • 21644440038 scopus 로고    scopus 로고
    • Yeast mRNA poly(A) tail length control can be reconstituted in vitro in the absence of Pab1p-dependent poly(A) nuclease activity
    • DOI 10.1074/jbc.M504720200
    • Dheur, S., Nykamp, K. R., Viphakone, N., Swanson, M. S., and Minvielle-Sebastia, L. (2005) Yeast mRNA Poly(A) tail length control can be reconstituted in vitro in the absence of Pab1p-dependent Poly(A) nuclease activity J. Biol. Chem. 280, 24532-24538 (Pubitemid 40934539)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24532-24538
    • Dheur, S.1    Nykamp, K.R.2    Viphakone, N.3    Swanson, M.S.4    Minvielle-Sebastia, L.5
  • 45
    • 79951536375 scopus 로고    scopus 로고
    • Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure
    • Moreno-Morcillo, M., Minvielle-Sébastia, L., Mackereth, C., and Fribourg, S. (2011) Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure RNA 17, 412-418
    • (2011) RNA , vol.17 , pp. 412-418
    • Moreno-Morcillo, M.1    Minvielle-Sébastia, L.2    MacKereth, C.3    Fribourg, S.4
  • 46
    • 79952459288 scopus 로고    scopus 로고
    • Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping
    • Yang, Q., Coseno, M., Gilmartin, G. M., and Doublié, S. (2011) Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping Structure 19, 368-377
    • (2011) Structure , vol.19 , pp. 368-377
    • Yang, Q.1    Coseno, M.2    Gilmartin, G.M.3    Doublié, S.4
  • 47
    • 79960138153 scopus 로고    scopus 로고
    • Structural basis of pre-mRNA recognition by the human cleavage factor I(m) complex
    • Li, H., Tong, S., Li, X., Shi, H., Ying, Z., Gao, Y., Ge, H., Niu, L., and Teng, M. (2011) Structural basis of pre-mRNA recognition by the human cleavage factor I(m) complex Cell Res. 21, 1039-1051
    • (2011) Cell Res. , vol.21 , pp. 1039-1051
    • Li, H.1    Tong, S.2    Li, X.3    Shi, H.4    Ying, Z.5    Gao, Y.6    Ge, H.7    Niu, L.8    Teng, M.9


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