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. 2001 Sep;7(9):1284–1297. doi: 10.1017/s1355838201016077

Evidence for a role of Sky1p-mediated phosphorylation in 3' splice site recognition involving both Prp8 and Prp17/Slu4.

S F Dagher 1, X D Fu 1
PMCID: PMC1370172  PMID: 11565750

Abstract

The SRPK family of kinases is specific for RS domain-containing splicing factors and known to play a critical role in protein-protein interaction and intracellular distribution of their substrates in both yeast and mammalian cells. However, the function of these kinases in pre-mRNA splicing remains unclear. Here we report that SKY1, a SRPK family member in Saccharomyces cerevisiae, genetically interacts with PRP8 and PRP17/SLU4, both of which are involved in splice site selection during pre-mRNA splicing. Prp8 is essential for splicing and is known to interact with both 5' and 3' splice sites in the spliceosomal catalytic center, whereas Prp17/Slu4 is nonessential and is required only for efficient recognition of the 3' splice site. Interestingly, deletion of SKY1 was synthetically lethal with all prp17 mutants tested, but only with specific prp8 alleles in a domain implicated in governing fidelity of 3'AG recognition. Indeed, deletion of SKY1 specifically suppressed 3'AG mutations in ACT1-CUP1 splicing reporters. These results suggest for the first time that 3' AG recognition may be subject to phosphorylation regulation by Sky1p during pre-mRNA splicing.

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Selected References

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  1. Abovich N., Rosbash M. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell. 1997 May 2;89(3):403–412. doi: 10.1016/s0092-8674(00)80221-4. [DOI] [PubMed] [Google Scholar]
  2. Ben Yehuda S., Dix I., Russell C. S., Levy S., Beggs J. D., Kupiec M. Identification and functional analysis of hPRP17, the human homologue of the PRP17/CDC40 yeast gene involved in splicing and cell cycle control. RNA. 1998 Oct;4(10):1304–1312. doi: 10.1017/s1355838298980712. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ben-Yehuda S., Russell C. S., Dix I., Beggs J. D., Kupiec M. Extensive genetic interactions between PRP8 and PRP17/CDC40, two yeast genes involved in pre-mRNA splicing and cell cycle progression. Genetics. 2000 Jan;154(1):61–71. doi: 10.1093/genetics/154.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Berglund J. A., Abovich N., Rosbash M. A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition. Genes Dev. 1998 Mar 15;12(6):858–867. doi: 10.1101/gad.12.6.858. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Berglund J. A., Chua K., Abovich N., Reed R., Rosbash M. The splicing factor BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC. Cell. 1997 May 30;89(5):781–787. doi: 10.1016/s0092-8674(00)80261-5. [DOI] [PubMed] [Google Scholar]
  6. Brown J. D., Beggs J. D. Roles of PRP8 protein in the assembly of splicing complexes. EMBO J. 1992 Oct;11(10):3721–3729. doi: 10.1002/j.1460-2075.1992.tb05457.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brys A., Schwer B. Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the distance between the branchpoint and the 3' splice site. RNA. 1996 Jul;2(7):707–717. [PMC free article] [PubMed] [Google Scholar]
  8. Cao W., Jamison S. F., Garcia-Blanco M. A. Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro. RNA. 1997 Dec;3(12):1456–1467. [PMC free article] [PubMed] [Google Scholar]
  9. Chanfreau G., Legrain P., Dujon B., Jacquier A. Interaction between the first and last nucleotides of pre-mRNA introns is a determinant of 3' splice site selection in S. cerevisiae. Nucleic Acids Res. 1994 Jun 11;22(11):1981–1987. doi: 10.1093/nar/22.11.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Chen J. Y., Stands L., Staley J. P., Jackups R. R., Jr, Latus L. J., Chang T. H. Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor. Mol Cell. 2001 Jan;7(1):227–232. doi: 10.1016/s1097-2765(01)00170-8. [DOI] [PubMed] [Google Scholar]
  11. Chew S. L., Liu H. X., Mayeda A., Krainer A. R. Evidence for the function of an exonic splicing enhancer after the first catalytic step of pre-mRNA splicing. Proc Natl Acad Sci U S A. 1999 Sep 14;96(19):10655–10660. doi: 10.1073/pnas.96.19.10655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Chiara M. D., Gozani O., Bennett M., Champion-Arnaud P., Palandjian L., 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. 1996 Jul;16(7):3317–3326. doi: 10.1128/mcb.16.7.3317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Chua K., Reed R. Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing. Genes Dev. 1999 Apr 1;13(7):841–850. doi: 10.1101/gad.13.7.841. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Chua K., Reed R. The RNA splicing factor hSlu7 is required for correct 3' splice-site choice. Nature. 1999 Nov 11;402(6758):207–210. doi: 10.1038/46086. [DOI] [PubMed] [Google Scholar]
  15. Collins C. A., Guthrie C. Allele-specific genetic interactions between Prp8 and RNA active site residues suggest a function for Prp8 at the catalytic core of the spliceosome. Genes Dev. 1999 Aug 1;13(15):1970–1982. doi: 10.1101/gad.13.15.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Collins C. A., Guthrie C. The question remains: is the spliceosome a ribozyme? Nat Struct Biol. 2000 Oct;7(10):850–854. doi: 10.1038/79598. [DOI] [PubMed] [Google Scholar]
  17. Colwill K., Feng L. L., Yeakley J. M., Gish G. D., Cáceres J. F., Pawson T., Fu X. D. SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. J Biol Chem. 1996 Oct 4;271(40):24569–24575. doi: 10.1074/jbc.271.40.24569. [DOI] [PubMed] [Google Scholar]
  18. Das R., Zhou Z., Reed R. Functional association of U2 snRNP with the ATP-independent spliceosomal complex E. Mol Cell. 2000 May;5(5):779–787. doi: 10.1016/s1097-2765(00)80318-4. [DOI] [PubMed] [Google Scholar]
  19. Deirdre A., Scadden J., Smith C. W. Interactions between the terminal bases of mammalian introns are retained in inosine-containing pre-mRNAs. EMBO J. 1995 Jul 3;14(13):3236–3246. doi: 10.1002/j.1460-2075.1995.tb07326.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Elledge S. J., Davis R. W. A family of versatile centromeric vectors designed for use in the sectoring-shuffle mutagenesis assay in Saccharomyces cerevisiae. Gene. 1988 Oct 30;70(2):303–312. doi: 10.1016/0378-1119(88)90202-8. [DOI] [PubMed] [Google Scholar]
  21. Frank D., Guthrie C. An essential splicing factor, SLU7, mediates 3' splice site choice in yeast. Genes Dev. 1992 Nov;6(11):2112–2124. doi: 10.1101/gad.6.11.2112. [DOI] [PubMed] [Google Scholar]
  22. Frank D., Patterson B., Guthrie C. Synthetic lethal mutations suggest interactions between U5 small nuclear RNA and four proteins required for the second step of splicing. Mol Cell Biol. 1992 Nov;12(11):5197–5205. doi: 10.1128/mcb.12.11.5197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Gilbert W., Siebel C. W., Guthrie C. Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. RNA. 2001 Feb;7(2):302–313. doi: 10.1017/s1355838201002369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Horowitz D. S., Abelson J. Stages in the second reaction of pre-mRNA splicing: the final step is ATP independent. Genes Dev. 1993 Feb;7(2):320–329. doi: 10.1101/gad.7.2.320. [DOI] [PubMed] [Google Scholar]
  25. Horowitz D. S., Krainer A. R. A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor. Genes Dev. 1997 Jan 1;11(1):139–151. doi: 10.1101/gad.11.1.139. [DOI] [PubMed] [Google Scholar]
  26. Jones M. H., Frank D. N., Guthrie C. Characterization and functional ordering of Slu7p and Prp17p during the second step of pre-mRNA splicing in yeast. Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9687–9691. doi: 10.1073/pnas.92.21.9687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Kandels-Lewis S., Séraphin B. Involvement of U6 snRNA in 5' splice site selection. Science. 1993 Dec 24;262(5142):2035–2039. doi: 10.1126/science.8266100. [DOI] [PubMed] [Google Scholar]
  28. Kistler A. L., Guthrie C. Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase. Genes Dev. 2001 Jan 1;15(1):42–49. doi: 10.1101/gad.851301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Kranz J. E., Holm C. Cloning by function: an alternative approach for identifying yeast homologs of genes from other organisms. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6629–6633. doi: 10.1073/pnas.87.17.6629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Krämer A. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu Rev Biochem. 1996;65:367–409. doi: 10.1146/annurev.bi.65.070196.002055. [DOI] [PubMed] [Google Scholar]
  31. Kuhn A. N., Brow D. A. Suppressors of a cold-sensitive mutation in yeast U4 RNA define five domains in the splicing factor Prp8 that influence spliceosome activation. Genetics. 2000 Aug;155(4):1667–1682. doi: 10.1093/genetics/155.4.1667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Kuhn A. N., Li Z., Brow D. A. Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome. Mol Cell. 1999 Jan;3(1):65–75. doi: 10.1016/s1097-2765(00)80175-6. [DOI] [PubMed] [Google Scholar]
  33. Lesser C. F., Guthrie C. Mutational analysis of pre-mRNA splicing in Saccharomyces cerevisiae using a sensitive new reporter gene, CUP1. Genetics. 1993 Apr;133(4):851–863. doi: 10.1093/genetics/133.4.851. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Libri D., Graziani N., Saguez C., Boulay J. Multiple roles for the yeast SUB2/yUAP56 gene in splicing. Genes Dev. 2001 Jan 1;15(1):36–41. doi: 10.1101/gad.852101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Lindsey L. A., Garcia-Blanco M. A. Functional conservation of the human homolog of the yeast pre-mRNA splicing factor Prp17p. J Biol Chem. 1998 Dec 4;273(49):32771–32775. doi: 10.1074/jbc.273.49.32771. [DOI] [PubMed] [Google Scholar]
  36. Lygerou Z., Christophides G., Séraphin B. A novel genetic screen for snRNP assembly factors in yeast identifies a conserved protein, Sad1p, also required for pre-mRNA splicing. Mol Cell Biol. 1999 Mar;19(3):2008–2020. doi: 10.1128/mcb.19.3.2008. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. MacMillan A. M., Query C. C., Allerson C. R., Chen S., Verdine G. L., Sharp P. A. Dynamic association of proteins with the pre-mRNA branch region. Genes Dev. 1994 Dec 15;8(24):3008–3020. doi: 10.1101/gad.8.24.3008. [DOI] [PubMed] [Google Scholar]
  38. Maroney P. A., Romfo C. M., Nilsen T. W. Functional recognition of 5' splice site by U4/U6.U5 tri-snRNP defines a novel ATP-dependent step in early spliceosome assembly. Mol Cell. 2000 Aug;6(2):317–328. doi: 10.1016/s1097-2765(00)00032-0. [DOI] [PubMed] [Google Scholar]
  39. McPheeters D. S., Schwer B., Muhlenkamp P. Interaction of the yeast DExH-box RNA helicase prp22p with the 3' splice site during the second step of nuclear pre-mRNA splicing. Nucleic Acids Res. 2000 Mar 15;28(6):1313–1321. doi: 10.1093/nar/28.6.1313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Merendino L., Guth S., Bilbao D., Martínez C., Valcárcel J. Inhibition of msl-2 splicing by Sex-lethal reveals interaction between U2AF35 and the 3' splice site AG. Nature. 1999 Dec 16;402(6763):838–841. doi: 10.1038/45602. [DOI] [PubMed] [Google Scholar]
  41. Mermoud J. E., Cohen P. T., Lamond A. I. Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J. 1994 Dec 1;13(23):5679–5688. doi: 10.1002/j.1460-2075.1994.tb06906.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Newman A. J., Norman C. U5 snRNA interacts with exon sequences at 5' and 3' splice sites. Cell. 1992 Feb 21;68(4):743–754. doi: 10.1016/0092-8674(92)90149-7. [DOI] [PubMed] [Google Scholar]
  43. Nolen B., Yun C. Y., Wong C. F., McCammon J. A., Fu X. D., Ghosh G. The structure of Sky1p reveals a novel mechanism for constitutive activity. Nat Struct Biol. 2001 Feb;8(2):176–183. doi: 10.1038/84178. [DOI] [PubMed] [Google Scholar]
  44. O'Keefe R. T., Newman A. J. Functional analysis of the U5 snRNA loop 1 in the second catalytic step of yeast pre-mRNA splicing. EMBO J. 1998 Jan 15;17(2):565–574. doi: 10.1093/emboj/17.2.565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Ohno M., Shimura Y. A human RNA helicase-like protein, HRH1, facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. Genes Dev. 1996 Apr 15;10(8):997–1007. doi: 10.1101/gad.10.8.997. [DOI] [PubMed] [Google Scholar]
  46. Parker R., Siliciano P. G. Evidence for an essential non-Watson-Crick interaction between the first and last nucleotides of a nuclear pre-mRNA intron. Nature. 1993 Feb 18;361(6413):660–662. doi: 10.1038/361660a0. [DOI] [PubMed] [Google Scholar]
  47. Prasad J., Colwill K., Pawson T., Manley J. L. The protein kinase Clk/Sty directly modulates SR protein activity: both hyper- and hypophosphorylation inhibit splicing. Mol Cell Biol. 1999 Oct;19(10):6991–7000. doi: 10.1128/mcb.19.10.6991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Puig O., Gottschalk A., Fabrizio P., Séraphin B. Interaction of the U1 snRNP with nonconserved intronic sequences affects 5' splice site selection. Genes Dev. 1999 Mar 1;13(5):569–580. doi: 10.1101/gad.13.5.569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Reed R. Mechanisms of fidelity in pre-mRNA splicing. Curr Opin Cell Biol. 2000 Jun;12(3):340–345. doi: 10.1016/s0955-0674(00)00097-1. [DOI] [PubMed] [Google Scholar]
  50. Reyes J. L., Kois P., Konforti B. B., Konarska M. M. The canonical GU dinucleotide at the 5' splice site is recognized by p220 of the U5 snRNP within the spliceosome. RNA. 1996 Mar;2(3):213–225. [PMC free article] [PubMed] [Google Scholar]
  51. Rose M. D., Broach J. R. Cloning genes by complementation in yeast. Methods Enzymol. 1991;194:195–230. doi: 10.1016/0076-6879(91)94017-7. [DOI] [PubMed] [Google Scholar]
  52. Schwelnus W., Richert K., Opitz F., Gross T., Habara Y., Tani T., Käufer N. F. Fission yeast Prp4p kinase regulates pre-mRNA splicing by phosphorylating a non-SR-splicing factor. EMBO Rep. 2001 Jan;2(1):35–41. doi: 10.1093/embo-reports/kve009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Schwer B., Gross C. H. Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. EMBO J. 1998 Apr 1;17(7):2086–2094. doi: 10.1093/emboj/17.7.2086. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Siatecka M., Reyes J. L., Konarska M. M. Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center. Genes Dev. 1999 Aug 1;13(15):1983–1993. doi: 10.1101/gad.13.15.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Siebel C. W., Feng L., Guthrie C., Fu X. D. Conservation in budding yeast of a kinase specific for SR splicing factors. Proc Natl Acad Sci U S A. 1999 May 11;96(10):5440–5445. doi: 10.1073/pnas.96.10.5440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Sontheimer E. J., Steitz J. A. The U5 and U6 small nuclear RNAs as active site components of the spliceosome. Science. 1993 Dec 24;262(5142):1989–1996. doi: 10.1126/science.8266094. [DOI] [PubMed] [Google Scholar]
  57. Staley J. P., Guthrie C. An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p. Mol Cell. 1999 Jan;3(1):55–64. doi: 10.1016/s1097-2765(00)80174-4. [DOI] [PubMed] [Google Scholar]
  58. Tang Z., Kuo T., Shen J., Lin R. J. Biochemical and genetic conservation of fission yeast Dsk1 and human SR protein-specific kinase 1. Mol Cell Biol. 2000 Feb;20(3):816–824. doi: 10.1128/mcb.20.3.816-824.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Tang Z., Yanagida M., Lin R. J. Fission yeast mitotic regulator Dsk1 is an SR protein-specific kinase. J Biol Chem. 1998 Mar 6;273(10):5963–5969. doi: 10.1074/jbc.273.10.5963. [DOI] [PubMed] [Google Scholar]
  60. Teigelkamp S., Newman A. J., Beggs J. D. Extensive interactions of PRP8 protein with the 5' and 3' splice sites during splicing suggest a role in stabilization of exon alignment by U5 snRNA. EMBO J. 1995 Jun 1;14(11):2602–2612. doi: 10.1002/j.1460-2075.1995.tb07258.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Umen J. G., Guthrie C. A novel role for a U5 snRNP protein in 3' splice site selection. Genes Dev. 1995 Apr 1;9(7):855–868. doi: 10.1101/gad.9.7.855. [DOI] [PubMed] [Google Scholar]
  62. Umen J. G., Guthrie C. Mutagenesis of the yeast gene PRP8 reveals domains governing the specificity and fidelity of 3' splice site selection. Genetics. 1996 Jun;143(2):723–739. doi: 10.1093/genetics/143.2.723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Umen J. G., Guthrie C. Prp16p, Slu7p, and Prp8p interact with the 3' splice site in two distinct stages during the second catalytic step of pre-mRNA splicing. RNA. 1995 Aug;1(6):584–597. [PMC free article] [PubMed] [Google Scholar]
  64. Vijayraghavan U., Company M., Abelson J. Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae. Genes Dev. 1989 Aug;3(8):1206–1216. doi: 10.1101/gad.3.8.1206. [DOI] [PubMed] [Google Scholar]
  65. Wang C., Chua K., Seghezzi W., Lees E., Gozani O., Reed R. Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis. Genes Dev. 1998 May 15;12(10):1409–1414. doi: 10.1101/gad.12.10.1409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Wang H. Y., Lin W., Dyck J. A., Yeakley J. M., Songyang Z., Cantley L. C., Fu X. D. SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. J Cell Biol. 1998 Feb 23;140(4):737–750. doi: 10.1083/jcb.140.4.737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Wu S., Romfo C. M., Nilsen T. W., Green M. R. Functional recognition of the 3' splice site AG by the splicing factor U2AF35. Nature. 1999 Dec 16;402(6763):832–835. doi: 10.1038/45590. [DOI] [PubMed] [Google Scholar]
  68. Wyatt J. R., Sontheimer E. J., Steitz J. A. Site-specific cross-linking of mammalian U5 snRNP to the 5' splice site before the first step of pre-mRNA splicing. Genes Dev. 1992 Dec;6(12B):2542–2553. doi: 10.1101/gad.6.12b.2542. [DOI] [PubMed] [Google Scholar]
  69. Xu D., Field D. J., Tang S. J., Moris A., Bobechko B. P., Friesen J. D. Synthetic lethality of yeast slt mutations with U2 small nuclear RNA mutations suggests functional interactions between U2 and U5 snRNPs that are important for both steps of pre-mRNA splicing. Mol Cell Biol. 1998 Apr;18(4):2055–2066. doi: 10.1128/mcb.18.4.2055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Yeakley J. M., Tronchère H., Olesen J., Dyck J. A., Wang H. Y., Fu X. D. Phosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors. J Cell Biol. 1999 May 3;145(3):447–455. doi: 10.1083/jcb.145.3.447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Yun C. Y., Fu X. D. Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J Cell Biol. 2000 Aug 21;150(4):707–718. doi: 10.1083/jcb.150.4.707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Zhang D., Rosbash M. Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex. Genes Dev. 1999 Mar 1;13(5):581–592. doi: 10.1101/gad.13.5.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Zhang M., Green M. R. Identification and characterization of yUAP/Sub2p, a yeast homolog of the essential human pre-mRNA splicing factor hUAP56. Genes Dev. 2001 Jan 1;15(1):30–35. doi: 10.1101/gad.851701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Zhang X., Schwer B. Functional and physical interaction between the yeast splicing factors Slu7 and Prp18. Nucleic Acids Res. 1997 Jun 1;25(11):2146–2152. doi: 10.1093/nar/25.11.2146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Zhou Z., Reed R. Human homologs of yeast prp16 and prp17 reveal conservation of the mechanism for catalytic step II of pre-mRNA splicing. EMBO J. 1998 Apr 1;17(7):2095–2106. doi: 10.1093/emboj/17.7.2095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Zorio D. A., Blumenthal T. Both subunits of U2AF recognize the 3' splice site in Caenorhabditis elegans. Nature. 1999 Dec 16;402(6763):835–838. doi: 10.1038/45597. [DOI] [PubMed] [Google Scholar]

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