References1 Mandel, CR, Bai, Y, Tong, L. Protein factors in pre‐mRNA 3′‐end processing. Cell Mol Life Sci 2008, 65:1099–1122. 2 Proudfoot, N. New perspectives on connecting messenger RNA 3′ end formation to transcription. Curr Opin Cell Biol 2004, 16:272–278. 3 Edmonds, M. A history of poly A sequences: from formation to factors to function. Prog Nucleic Acid Res Mol Biol 2002, 71:285–389. 4 Zhao, J, Hyman, L, Moore, C. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol Mol Biol Rev 1999, 63:405–445. 5 Danckwardt, S, Hentze, MW, Kulozik, AE. 3′ end mRNA processing: molecular mechanisms and implications for health and disease. EMBO J 2008, 27:482–498. 6 Wahle, E, Ruegsegger, U. 3′‐End processing of pre‐mRNA in eukaryotes. FEMS Microbiol Rev 1999, 23:277–295. 7 Dominski, Z, Marzluff, WF. Formation of the 3′ end of histone mRNA. Gene 1999, 239:1–14. 8 Proudfoot, N, O`Sullivan, J. Polyadenylation: a tail of two complexes. Curr Biol 2002, 12:R855–R857. 9 Shi, Y, Di Giammartino, DC, Taylor, D, Sarkeshik, A, Rice, WJ, Yates, JR 3rd, Frank, J, Manley, JL. Molecular architecture of the human pre‐mRNA 3′ processing complex. Mol Cell 2009, 33:365–376. 10 Moore, MJ, Proudfoot, NJ. Pre‐mRNA processing reaches back to transcription and ahead to translation. Cell 2009, 136:688–700. 11 Millevoi, S, Vagner, S. Molecular mechanisms of eukaryotic pre‐mRNA 3′ end processing regulation. Nucleic Acids Res 2010, 38:2757–2774. 12 Lutz, CS. Alternative polyadenylation: a twist on mRNA 3′ end formation. ACS Chem Biol 2008, 3:609–617. 13 Hunt, AG. Messenger RNA 3′ end formation in plants. Curr Top Microbiol Immunol 2008, 326:151–177. 14 Ji, Z, Lee, JY, Pan, Z, Jiang, B, Tian, B. Progressive lengthening of 3′ untranslated regions of mRNAs by alternative polyadenylation during mouse embryonic development. Proc Natl Acad Sci U S A 2009, 106:7028–7033. 15 Tian, B, Hu, J, Zhang, H, Lutz, CS. A large‐scale analysis of mRNA polyadenylation of human and mouse genes. Nucleic Acids Res 2005, 33:201–212. 16 Shi, Y, Chan, S, Martinez‐Santibanez, G. An up‐close look at the pre‐mRNA 3′‐end processing complex. RNA Biol 2009, 6:522–525. 17 Gilmartin, GM. Eukaryotic mRNA 3′ processing: a common means to different ends. Genes Dev 2005, 19:2517–2521. 18 Lutz, CS, Moreira, A. Alternative mRNA polyadenylation in eukaryotes: an effective regulator of gene expression. WIREs RNA 2011, 2:22–31. 19 Chan, S, Choi, E‐A, Shi, Y. Pre‐mRNA 3′‐end processing complex assembly and function. WIRES RNA 2011, 3:321–335. 20 Kaufmann, I, Martin, G, Friedlein, A, Langen, H, Keller, W. Human Fip1 is a subunit of CPSF that binds to U‐rich RNA elements and stimulates poly(A) polymerase. EMBO J 2004, 23:616–626. 21 Rüegsegger, U, Blank, D, Keller, W. Human pre‐mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. Mol Cell 1998, 1:243–253. 22 Barabino, SM, Hubner, W, Jenny, A, Minvielle‐Sebastia, L, Keller, W. The 30‐kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA‐binding zinc finger proteins. Genes Dev 1997, 11:1703–1716. 23 Rüegsegger, U, Beyer, K, Keller, W. Purification and characterization of human cleavage factor Im involved in the 3′ end processing of messenger RNA precursors. J Biol Chem 1996, 271:6107–6113. 24 Kessler, MM, Zhao, J, Moore, CL. 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 1996, 271:27167–27175. 25 Murthy, KG, Manley, JL. The 160‐kD subunit of human cleavage‐polyadenylation specificity factor coordinates pre‐mRNA 3′‐end formation. Genes Dev 1995, 9:2672–2683. 26 Minvielle‐Sebastia, L, Preker, PJ, Keller, W. RNA14 and RNA15 proteins as components of a yeast pre‐mRNA 3′‐end processing factor. Science 1994, 266:1702–1705. 27 MacDonald, CC, Wilusz, J, Shenk, T. The 64‐kilodalton subunit of the CstF polyadenylation factor binds to pre‐mRNAs downstream of the cleavage site and influences cleavage site location. Mol Cell Biol 1994, 14:6647–6654. 28 Coseno, M, Martin, G, Berger, C, Gilmartin, G, Keller, W, Doublié, S. Crystal structure of the 25 kDa subunit of human cleavage factor Im. Nucleic Acids Res 2008, 36:3474–3483. 29 Tresaugues, L, Stenmark, P, Schuler, H, Flodin, S, Welin, M, Nyman, T, Hammarstrom, M, Moche, M, Graslund, S, Nordlund, P. The crystal structure of human cleavage and polyadenylation specific factor‐5 reveals a dimeric Nudix protein with a conserved catalytic site. Proteins 2008, 73:1047–1052. 30 Mandel, CR, Kaneko, S, Zhang, H, Gebauer, D, Vethantham, V, Manley, JL, Tong, L. Polyadenylation factor CPSF‐73 is the pre‐mRNA 3′‐end‐processing endonuclease. Nature 2006, 444:953–956. 31 Nishida, Y, Ishikawa, H, Baba, S, Nakagawa, N, Kuramitsu, S, Masui, R. Crystal structure of an archaeal cleavage and polyadenylation specificity factor subunit from Pyrococcus horikoshii. Proteins 2010, 78:2395–2398. 32 Mir‐Montazeri, B, Ammelburg, M, Forouzan, D, Lupas, AN, Hartmann, MD. Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor. J Struct Biol 2011, 173:191–195. 33 Perez Canadillas, JM, Varani, G. Recognition of GU‐rich polyadenylation regulatory elements by human CstF‐64 protein. EMBO J 2003, 22:2821–2830. 34 Pancevac, C, Goldstone, DC, Ramos, A, Taylor, IA. Structure of the Rna15 RRM‐RNA complex reveals the molecular basis of GU specificity in transcriptional 3′‐end processing factors. Nucleic Acids Res 2010, 38:3119–3132. 35 Qu, X, Perez‐Canadillas, JM, Agrawal, S, De Baecke, J, Cheng, H, Varani, G, Moore, C. 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 2007, 282:2101–2115. 36 Legrand, P, Pinaud, N, Minvielle‐Sebastia, L, Fribourg, S. The structure of the CstF‐77 homodimer provides insights into CstF assembly. Nucleic Acids Res 2007, 35:4515–4522. 37 Bai, Y, Auperin, TC, Chou, CY, Chang, GG, Manley, JL, Tong, L. Crystal structure of murine CstF‐77: dimeric association and implications for polyadenylation of mRNA precursors. Mol Cell 2007, 25:863–875. 38 Moreno‐Morcillo, M, Minvielle‐Sebastia, L, Mackereth, C, Fribourg, S. Hexameric architecture of CstF supported by CstF‐50 homodimerization domain structure. RNA 2011, 17:412–418. 39 Kennedy, SA, Frazier, ML, Steiniger, M, Mast, AM, Marzluff, WF, Redinbo, MR. Crystal structure of the HEAT domain from the Pre‐mRNA processing factor Symplekin. J Mol Biol 2009, 392:115–128. 40 Noble, CG, Hollingworth, D, Martin, SR, Ennis‐Adeniran, V, Smerdon, SJ, Kelly, G, Taylor, IA, Ramos, A. Key features of the interaction between Pcf11 CID and RNA polymerase II CTD. Nat Struct Mol Biol 2005, 12:144–151. 41 Meinhart, A, Cramer, P. Recognition of RNA polymerase II carboxy‐terminal domain by 3′‐RNA‐processing factors. Nature 2004, 430:223–226. 42 Martin, G, Keller, W, Doublié, S. Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J 2000, 19:4193–4203. 43 Martin, G, Moglich, A, Keller, W, Doublié, S. Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase. J Mol Biol 2004, 341:911–925. 44 Bard, J, Zhelkovsky, AM, Helmling, S, Earnest, TN, Moore, CL, Bohm, A. Structure of yeast poly(A) polymerase alone and in complex with 3′‐dATP. Science 2000, 289:1346–1349. 45 Balbo, PB, Toth, J, Bohm, A. X‐ray crystallographic and steady state fluorescence characterization of the protein dynamics of yeast polyadenylate polymerase. J Mol Biol 2007, 366:1401–1415. 46 Ge, H, Zhou, D, Tong, S, Gao, Y, Teng, M, Niu, L. Crystal structure and possible dimerization of the single RRM of human PABPN1. Proteins 2008, 71:1539–1545. 47 Yang, Q, Coseno, M, Gilmartin, GM, Doublié, S. Crystal structure of a human cleavage factor CFIm25/CFIm68/RNA complex provides an insight into poly(A) site recognition and rna looping. Structure 2011, 19:368–377. 48 Das, K, Ma, LC, Xiao, R, Radvansky, B, Aramini, J, Zhao, L, Marklund, J, Kuo, RL, Twu, KY, Arnold, E, et al. Structural basis for suppression of a host antiviral response by influenza A virus. Proc Natl Acad Sci U S A 2008, 105:13093–13098. 49 Noble, CG, Beuth, B, Taylor, IA. Structure of a nucleotide‐bound Clp1‐Pcf11 polyadenylation factor. Nucleic Acids Res 2007, 35:87–99. 50 Meinke, G, Ezeokonkwo, C, Balbo, P, Stafford, W, Moore, C, Bohm, A. Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. Biochemistry 2008, 47:6859–6869. 51 Xiang, K, Nagaike, T, Xiang, S, Kilic, T, Beh, MM, Manley, JL, Tong, L. Crystal structure of the human symplekin‐Ssu72‐CTD phosphopeptide complex. Nature 2010, 467: 729–733. 52 Yang, Q, Gilmartin, GM, Doublié, S. Structural basis of UGUA recognition by the Nudix protein CFIm25 and implications for a regulatory role in mRNA 3′ processing. Proc Natl Acad Sci U S A 2010, 107:10062–10067. 53 Perez‐Canadillas, JM. Grabbing the message: structural basis of mRNA 3′UTR recognition by Hrp1. EMBO J 2006, 25:3167–3178. 54 Leeper, TC, Qu, X, Lu, C, Moore, C, Varani, G. Novel protein‐protein contacts facilitate mRNA 3′‐processing signal recognition by Rna15 and Hrp1. J Mol Biol 2010, 401:334–349. 55 Balbo, PB, Bohm, A. Mechanism of poly(A) polymerase: structure of the enzyme‐MgATP‐RNA ternary complex and kinetic analysis. Structure 2007, 15: 1117–1131. 56 Deo, RC, Bonanno, JB, Sonenberg, N, Burley, SK. Recognition of polyadenylate RNA by the poly(A)‐binding protein. Cell 1999, 98:835–845. 57 Venkataraman, K, Brown, KM, Gilmartin, GM. Analysis of a noncanonical poly(A) site reveals a tripartite mechanism for vertebrate poly(A) site recognition. Genes Dev 2005, 19:1315–1327. 58 Proudfoot, NJ, Brownlee, GG. 3′ non‐coding region sequences in eukaryotic messenger RNA. Nature 1976, 263:211–214. 59 Beaudoing, E, Freier, S, Wyatt, JR, Claverie, JM, Gautheret, D. Patterns of variant polyadenylation signal usage in human genes. Genome Res 2000, 10:1001–1010. 60 Hu, J, Lutz, CS, Wilusz, J, Tian, B. Bioinformatic identification of candidate cis‐regulatory elements involved in human mRNA polyadenylation. RNA 2005, 11:1485–1493. 61 Shen, Y, Ji, G, Haas, BJ, Wu, X, Zheng, J, Reese, GJ, Li, QQ. Genome level analysis of rice mRNA 3′‐end processing signals and alternative polyadenylation. Nucleic Acids Res 2008, 36:3150–3161. 62 Fitzgerald, M, Shenk, T. The sequence 5′‐AAUAAA‐3′ forms parts of the recognition site for polyadenylation of late SV40 mRNAs. Cell 1981, 24:251–260. 63 Salisbury, J, Hutchison, KW, Graber, JH. A multispecies comparison of the metazoan 3′‐processing downstream elements and the CstF‐64 RNA recognition motif. BMC Genomics 2006, 7:55. 64 Graber, JH, Cantor, CR, Mohr, SC, Smith, TF. Genomic detection of new yeast pre‐mRNA 3′‐end‐processing signals. Nucleic Acids Res 1999, 27:888–894. 65 Kessler, MM, Henry, MF, Shen, E, Zhao, J, Gross, S, Silver, PA, Moore, CL. Hrp1, a sequence‐specific RNA‐binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′‐end formation in yeast. Genes Dev 1997, 11:2545–2556. 66 Dichtl, B, Keller, W. Recognition of polyadenylation sites in yeast pre‐mRNAs by cleavage and polyadenylation factor. EMBO J 2001, 20:3197–3209. 67 Ruepp, MD, Schümperli, D, Barabino, SML. mRNA 3′ end processing and more—multiple functions of mammalian cleavage factor I‐68. WIREs RNA 2011, 2:79–91. 68 Takagaki, Y, Ryner, LC, Manley, JL. Separation and characterization of a poly(A) polymerase and a cleavage/specificity factor required for pre‐mRNA polyadenylation. Cell 1988, 52:731–742. 69 Brown, KM, Gilmartin, GM. A mechanism for the regulation of pre‐mRNA 3′ processing by human cleavage factor Im. Mol Cell 2003, 12:1467–1476. 70 Dettwiler, S, Aringhieri, C, Cardinale, S, Keller, W, Barabino, SM. Distinct sequence motifs within the 68‐kDa subunit of cleavage factor Im mediate RNA binding, protein‐protein interactions, and subcellular localization. J Biol Chem 2004, 279:35788–35797. 71 McLennan, AG. The Nudix hydrolase superfamily. Cell Mol Life Sci 2006, 63:123–143. 72 Mildvan, AS, Xia, Z, Azurmendi, HF, Saraswat, V, Legler, PM, Massiah, MA, Gabelli, SB, Bianchet, MA, Kang, LW, Amzel, LM. Structures and mechanisms of Nudix hydrolases. Arch Biochem Biophys 2005, 433:129–143. 73 Auweter, SD, Fasan, R, Reymond, L, Underwood, JG, Black, DL, Pitsch, S, Allain, FH. Molecular basis of RNA recognition by the human alternative splicing factor Fox‐1. EMBO J 2006, 25:163–173. 74 Kim, H, Lee, Y. Interaction of poly(A) polymerase with the 25‐kDa subunit of cleavage factor I. Biochem Biophys Res Commun 2001, 289:513–518. 75 Shimazu, T, Horinouchi, S, Yoshida, M. Multiple histone deacetylases and the CREB‐binding protein regulate pre‐mRNA 3′‐end processing. J Biol Chem 2007, 282:4470–4478. 76 Graveley, BR. Sorting out the complexity of SR protein functions. RNA 2000, 6:1197–1211. 77 Millevoi, S, Loulergue, C, Dettwiler, S, Karaa, SZ, Keller, W, Antoniou, M, Vagner, S. An interaction between U2AF 65 and CF I(m) links the splicing and 3′ end processing machineries. EMBO J 2006, 25:4854–4864. 78 Awasthi, S, Alwine, JC. Association of polyadenylation cleavage factor I with U1 snRNP. RNA 2003, 9:1400–1409. 79 Rappsilber, J, Ryder, U, Lamond, AI, Mann, M. Large‐scale proteomic analysis of the human spliceosome. Genome Res 2002, 12:1231–1245. 80 Zhou, Z, Sim, J, Griffith, J, Reed, R. Purification and electron microscopic visualization of functional human spliceosomes. Proc Natl Acad Sci U S A 2002, 99:12203–12207. 81 Clery, A, Blatter, M, Allain, FH. RNA recognition motifs: boring? Not quite. Curr Opin Struct Biol 2008, 18:290–298. 82 Kubo, T, Wada, T, Yamaguchi, Y, Shimizu, A, Handa, H. Knock‐down of 25 kDa subunit of cleavage factor Im in Hela cells alters alternative polyadenylation within 3′‐UTRs. Nucleic Acids Res 2006, 34:6264–6271. 83 Sartini, BL, Wang, H, Wang, W, Millette, CF, Kilpatrick, DL. Pre‐messenger RNA cleavage factor I (CFIm): potential role in alternative polyadenylation during spermatogenesis. Biol Reprod 2008, 78:472–482. 84 Ruepp, MD, Aringhieri, C, Vivarelli, S, Cardinale, S, Paro, S, Schumperli, D, Barabino, SM. Mammalian pre‐mRNA 3′ end processing factor CF I m 68 functions in mRNA export. Mol Biol Cell 2009, 20:5211–5223. 85 Sullivan, KD, Steiniger, M, Marzluff, WF. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol Cell 2009, 34:322–332. 86 Ryan, K, Calvo, O, Manley, JL. Evidence that polyadenylation factor CPSF‐73 is the mRNA 3′ processing endonuclease. RNA 2004, 10:565–573. 87 Callebaut, I, Moshous, D, Mornon, JP, de Villartay, JP. Metallo‐ β‐lactamase fold within nucleic acids processing enzymes: the β‐CASP family. Nucleic Acids Res 2002, 30:3592–3601. 88 Neuwald, AF, Liu, JS, Lipman, DJ, Lawrence, CE. Extracting protein alignment models from the sequence database. Nucleic Acids Res 1997, 25: 1665–1677. 89 Dominski, Z. Nucleases of the metallo‐ β‐lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol 2007, 42:67–93. 90 Ishikawa, H, Nakagawa, N, Kuramitsu, S, Masui, R. Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo‐ β‐lactamase superfamily. J Biochem 2006, 140:535–542. 91 de la Sierra‐Gallay, IL, Zig, L, Jamalli, A, Putzer, H. Structural insights into the dual activity of RNase J. Nat Struct Mol Biol 2008, 15:206–212. 92 Bebrone, C. Metallo‐ β‐lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem Pharmacol 2007, 74:1686–1701. 93 Kolev, NG, Yario, TA, Benson, E, Steitz, JA. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation. EMBO Rep 2008, 9:1013–1018. 94 Auweter, SD, Oberstrass, FC, Allain, FH. Sequence‐specific binding of single‐stranded RNA: is there a code for recognition? Nucleic Acids Res 2006, 34:4943–4959. 95 Castro, C, Smidansky, ED, Arnold, JJ, Maksimchuk, KR, Moustafa, I, Uchida, A, Gotte, M, Konigsberg, W, Cameron, CE. Nucleic acid polymerases use a general acid for nucleotidyl transfer. Nat Struct Mol Biol 2009, 16:212–218. 96 Kyburz, A, Sadowski, M, Dichtl, B, Keller, W. The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre‐mRNA 3′‐end formation. Nucleic Acids Res 2003, 31:3936–3945. 97 Xu, R, Zhao, H, Dinkins, RD, Cheng, X, Carberry, G, Li, QQ. The 73 kD subunit of the cleavage and polyadenylation specificity factor (CPSF) complex affects reproductive development in Arabidopsis. Plant Mol Biol 2006, 61:799–815. 98 Dominski, Z, Yang, XC, Purdy, M, Wagner, EJ, Marzluff, WF. A CPSF‐73 homologue is required for cell cycle progression but not cell growth and interacts with a protein having features of CPSF‐100. Mol Cell Biol 2005, 25:1489–1500. 99 Yang, XC, Sullivan, KD, Marzluff, WF, Dominski, Z. Studies of the 5′ exonuclease and endonuclease activities of CPSF‐73 in histone pre‐mRNA processing. Mol Cell Biol 2009, 29:31–42. 100 Moore, CL, Chen, J, Whoriskey, J. Two proteins crosslinked to RNA containing the adenovirus L3 poly(A) site require the AAUAAA sequence for binding. EMBO J 1988, 7:3159–3169. 101 Dichtl, B, Blank, D, Sadowski, M, Hubner, W, Weiser, S, Keller, W. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. EMBO J 2002, 21:4125–4135. 102 Barabino, SM, Ohnacker, M, Keller, W. Distinct roles of two Yth1p domains in 3′‐end cleavage and polyadenylation of yeast pre‐mRNAs. EMBO J 2000, 19:3778–3787. 103 Chen, Z, Li, Y, Krug, RM. Influenza A virus NS1 protein targets poly(A)‐binding protein II of the cellular 3′‐end processing machinery. EMBO J 1999, 18:2273–2283. 104 Wilusz, J, Shenk, T, Takagaki, Y, Manley, JL. A multicomponent complex is required for the AAUAAA‐dependent cross‐linking of a 64‐kilodalton protein to polyadenylation substrates. Mol Cell Biol 1990, 10:1244–1248. 105 Takagaki, Y, Manley, JL. A polyadenylation factor subunit is the human homologue of the Drosophila suppressor of forked protein. Nature 1994, 372:471–474. 106 Wahle, E, Lustig, A, Jeno, P, Maurer, P. Mammalian poly(A)‐binding protein II. Physical properties and binding to polynucleotides. J Biol Chem 1993, 268:2937–2945. 107 Moreira, A, Takagaki, Y, Brackenridge, S, Wollerton, M, Manley, JL, Proudfoot, NJ. The upstream sequence element of the C2 complement poly(A) signal activates mRNA 3′ end formation by two distinct mechanisms. Genes Dev 1998, 12:2522–2534. 108 Takagaki, Y, Manley, JL. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol Cell Biol 2000, 20:1515–1525. 109 Wilusz, J, Shenk, T. A 64 kd nuclear protein binds to RNA segments that include the AAUAAA polyadenylation motif. Cell 1988, 52:221–228. 110 Gilmartin, GM, Nevins, JR. Molecular analyses of two poly(A) site‐processing factors that determine the recognition and efficiency of cleavage of the pre‐mRNA. Mol Cell Biol 1991, 11:2432–2438. 111 Deka, P, Rajan, PK, Perez‐Canadillas, JM, Varani, G. Protein and RNA dynamics play key roles in determining the specific recognition of GU‐rich polyadenylation regulatory elements by human Cstf‐64 protein. J Mol Biol 2005, 347:719–733. 112 Beyer, K, Dandekar, T, Keller, W. RNA ligands selected by cleavage stimulation factor contain distinct sequence motifs that function as downstream elements in 3′‐end processing of pre‐mRNA. J Biol Chem 1997, 272:26769–26779. 113 Takagaki, Y, Manley, JL. RNA recognition by the human polyadenylation factor CstF. Mol Cell Biol 1997, 17:3907–3914. 114 Vander Kooi, CW, Ren, L, Xu, P, Ohi, MD, Gould, KL, Chazin, WJ. The Prp19 WD40 domain contains a conserved protein interaction region essential for its function. Structure 2010, 18:584–593. 115 Rose, R, Weyand, M, Lammers, M, Ishizaki, T, Ahmadian, MR, Wittinghofer, A. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 2005, 435:513–518. 116 Ye, K, Patel, DJ. RNA silencing suppressor p21 of Beet yellows virus forms an RNA binding octameric ring structure. Structure 2005, 13:1375–1384. 117 Hatton, LS, Eloranta, JJ, Figueiredo, LM, Takagaki, Y, Manley, JL, O`Hare, K. The Drosophila homologue of the 64 kDa subunit of cleavage stimulation factor interacts with the 77 kDa subunit encoded by the suppressor of forked gene. Nucleic Acids Res 2000, 28:520–526. 118 Hockert, JA, Yeh, HJ, MacDonald, CC. The hinge domain of the cleavage stimulation factor protein CstF‐64 is essential for CstF‐77 interaction, nuclear localization, and polyadenylation. J Biol Chem 2010, 285:695–704. 119 Lamb, JR, Tugendreich, S, Hieter, P. Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem Sci 1995, 20:257–259. 120 Preker, PJ, Keller, W. The HAT helix, a repetitive motif implicated in RNA processing. Trends Biochem Sci 1998, 23:15–16. 121 Gatto, GJ Jr, Geisbrecht, BV, Gould, SJ, Berg, JM. Peroxisomal targeting signal‐1 recognition by the TPR domains of human PEX5. Nat Struct Biol 2000, 7:1091–1095. 122 Noble, CG, Walker, PA, Calder, LJ, Taylor, IA. Rna14‐Rna15 assembly mediates the RNA‐binding capability of Saccharomyces cerevisiae cleavage factor IA. Nucleic Acids Res 2004, 32:3364–3375. 123 Bell, SA, Hunt, AG. The Arabidopsis ortholog of the 77 kDa subunit of the cleavage stimulatory factor (AtCstF‐77) involved in mRNA polyadenylation is an RNA‐binding protein. FEBS Lett 2010, 584:1449–1454. 124 Takagaki, Y, Manley, JL. A human polyadenylation factor is a G protein β‐subunit homologue. J Biol Chem 1992, 267:23471–23474. 125 Li, D, Roberts, R. WD‐repeat proteins: structure characteristics, biological function, and their involvement in human diseases. Cell Mol Life Sci 2001, 58:2085–2097. 126 Smith, TF, Gaitatzes, C, Saxena, K, Neer, EJ. The WD repeat: a common architecture for diverse functions. Trends Biochem Sci 1999, 24:181–185. 127 Couture, JF, Collazo, E, Trievel, RC. Molecular recognition of histone H3 by the WD40 protein WDR5. Nat Struct Mol Biol 2006, 13:698–703. 128 Kleiman, FE, Manley, JL. The BARD1‐CstF‐50 interaction links mRNA 3′ end formation to DNA damage and tumor suppression. Cell 2001, 104:743–753. 129 Kleiman, FE, Manley, JL. Functional interaction of BRCA1‐associated BARD1 with polyadenylation factor CstF‐50. Science 1999, 285:1576–1579. 130 Edwards, RA, Lee, MS, Tsutakawa, SE, Williams, RS, Nazeer, I, Kleiman, FE, Tainer, JA, Glover, JN. The BARD1 C‐terminal domain structure and interactions with polyadenylation factor CstF‐50. Biochemistry 2008, 47:11446–11456. 131 Scully, R, Xie, A, Nagaraju, G. Molecular functions of BRCA1 in the DNA damage response. Cancer Biol Ther 2004, 3:521–527. 132 Ohnacker, M, Barabino, SM, Preker, PJ, Keller, W. The WD‐repeat protein pfs2p bridges two essential factors within the yeast pre‐mRNA 3′‐end‐processing complex. EMBO J 2000, 19:37–47. 133 McCracken, S, Fong, N, Yankulov, K, Ballantyne, S, Pan, G, Greenblatt, J, Patterson, SD, Wickens, M, Bentley, DL. The C‐terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 1997, 385:357–361. 134 Minvielle‐Sebastia, L, Beyer, K, Krecic, AM, Hector, RE, Swanson, MS, Keller, W. Control of cleavage site selection during mRNA 3′ end formation by a yeast hnRNP. EMBO J 1998, 17:7454–7468. 135 Gross, S, Moore, C. 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 2001, 98:6080–6085. 136 Valentini, SR, Weiss, VH, Silver, PA. Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3′‐end formation. RNA 1999, 5:272–280. 137 Chen, S, Hyman, LE. A specific RNA‐protein interaction at yeast polyadenylation efficiency elements. Nucleic Acids Res 1998, 26:4965–4974. 138 Gross, S, Moore, CL. Rna15 interaction with the A‐rich yeast polyadenylation signal is an essential step in mRNA 3′‐end formation. Mol Cell Biol 2001, 21:8045–8055. 139 Kim Guisbert, KS, Li, H, Guthrie, C. Alternative 3′ pre‐mRNA processing in Saccharomyces cerevisiae is modulated by Nab4/Hrp1 in vivo. PLoS Biol 2007, 5:e6.