Mechanisms of fidelity in pre-mRNA splicing

Current Opinion in Cell Biology

Volumn 12, Issue 3, 2000, Pages 340-345

  Reed, Robin ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DINUCLEOTIDE; MESSENGER RNA; NUCLEAR PROTEIN; NUCLEAR RNA;

CATALYSIS; HUMAN; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; REVIEW; RNA SPLICING; SPLICEOSOME;

EID: 0034069505     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00097-1     Document Type: Review

References (44)

1. Reed R. Initial splice-site recognition and pairing during pre-mRNA splicing. Curr Opin Genet Dev. 6:1996;215-220.
2. Burge C.B., Tuschl T.H., Sharp P. Splicing of precursors to mRNAs by the spliceosome. Gesteland R.F., Cech T.R., Atkins J.F. In RNA World II. 1998;525-560 Cold Spring Harbor Laboratory Press, New York.
3. Staley J.P., Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell. 92:1998;315-326.
4. Tacke R., Manley J.L. Determinants of SR protein specificity. Curr Opin Cell Biol. 11:1999;358-362.
5. Wu Q., Krainer A.R. AT-AC pre-mRNA splicing mechanisms and conservation of minor introns in voltage-gated ion channel genes. Mol Cell Biol. 19:1999;3225-3236.
6. Minvielle-Sebastia L., Keller W. mRNA polyadenylation and its coupling to other RNA processing reactions and to transcription. Curr Opin Cell Biol. 11:1999;352-357.
7. Kambach C., Walke S., Nagai K. Structure and assembly of the spliceosomal small nuclear ribonucleoprotein particles. Curr Opin Struct Biol. 9:1999;222-230.
8. Zhang D., Rosbash M. Identification of eight proteins that cross link to pre-mRNA in the yeast commitment complex. Genes Dev. 13:1999;581-592. An RNA-protein crosslinking assay reveals the first proteins that interact in the vicinity of the 5′ splice site in the yeast commitment complex. These proteins are likely to mediate U1 snRNA-5′ splice site interactions.
9. Puig O., Gottschalk A., Fabrizio P., Seraphin B. Interaction of the U1 snRNP with nonconserved intronic sequences affects 5′ splice site selection. Genes Dev. 13:1999;569-580. The U1 snRNP protein Nam8 is shown to be a component of commitment complex, to crosslink to pre-RNA near the 5′ splice site, and to affect 5′ splice-site choice.
10. Abovich N., Rosbash M. Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell. 89:1997;403-412.
11. Wu J.Y., Maniatis T. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell. 75:1993;1061-1070.
12. Hertel K.J., Maniatis T. Serine-arginine (SR)-rich splicing factors have an exon-independent function in pre-mRNA splicing. Proc Natl Acad Sci USA. 96:1999;2651-2655.
13. Zuo P., Maniatis T. The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. Genes Dev. 10:1996;1356-1368.
14. Guth S., Martinez C., Gaur R.K., Valcarcel J. Evidence for substrate-specific requirement of the splicing factor U2AF(35) and for its function after polypyrimidine tract recognition by U2AF(65). Mol Cell Biol. 19:1999;8263-8271.
15. 35 specifically requires the AG dinucleotide.
16. 35 is shown to be the factor that functionally recognizes the AG dinucleotide at the 3′ splice site early in spliceosome assembly.
17. 35 recognizes the AG at the 3′ splice site.
18. Berget S.M. Exon recognition in vertebrate splicing. J Biol Chem. 270:1995;2411-2414.
19. Schaal T.D., Maniatis T. Multiple distinct splicing enhancers in the protein-coding sequences of a constitutively spliced pre-mRNA. Mol Cell Biol. 19:1999;261-273.
20. Mayeda A., Screaton G.R., Chandler S.D., Fu X.D., Krainer A.R. Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements. Mol Cell Biol. 19:1999;1853-1863.
21. Caputi M., Mayeda A., Krainer A.R., Zahler A.M. hnRNP A/B proteins are required for inhibition of HIV-1 pre-mRNA splicing. EMBO J. 18:1999;4060-4067.
22. Del Gatto-Konczak F., Olive M., Gesnel M.C., Breathnach R. hnRNP A1 recruited to an exon in vivo can function as an exon splicing silencer. Mol Cell Biol. 19:1999;251-260.
23. Kan J.L., Green M.R. Pre-mRNA splicing of IgM exons M1 and M2 is directed by a juxtaposed splicing enhancer and inhibitor. Genes Dev. 13:1999;462-471.
24. Chen C.D., Kobayashi D.M., Helfman R. Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-tropomyosin gene. Genes Dev. 13:1999;593-606.
25. Dreyfuss G., Matunis M.J., Pinol-Roma S., Burd C.G. hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem. 62:1993;289-321.
26. Kramer A. The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu Rev Biochem. 65:1996;367-409.
27. Kramer A., Gruter P., Groning K., Kastner B. Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP. J Cell Biol. 145:1999;1355-1368.
28. Das B.K., Xia L., Palandjian L., Gozani O., Chyung Y., Reed R. Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol Cell Biol. 19:1999;6796-6802.
29. Mintz P.J., Patterson S.D., Neuwald A.F., Spahr C.S., Spector D.L. Purification and biochemical characterization of interchromatin granule clusters. EMBO J. 18:1999;4308-4320.
30. Caspary F., Shevchenko A., Wilm M., Seraphin B. Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assembly. EMBO J. 18:1999;3463-3474.
31. Chen E.J., Frand A.R., Chitouras E., Kaiser C.A. A link between secretion and pre-mRNA processing defects in Saccharomyces cerevisiae and the identification of a novel splicing gene, RSE1. Mol Cell Biol. 18:1998;7139-7146.
32. Will C.L., Schneider C., Reed R., Luhrmann R. Identification of both shared and distinct proteins in the major and minor spliceosomes. Science. 284:1999;2003-2005.
33. Frilander M.J., 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. U11 and U12 were found to bind simultaneously to the 5′ splice site and branch site, respectively, during A complex assembly. This is in contrast to A complex assembly in yeast and metazoans in which U1 and U2 binding is thought to occur sequentially.
34. Staley J.P., Guthrie C. An RNA switch at the 5′ splice site requires ATP and the DEAD box protein Prp28p. Mol Cell. 3:1999;55-64. The duplex between U1 snRNA and the 5′ splice site was lengthened, which resulted in a block of the switch of U1 for U6 snRNA at the 5′ splice site. The ATPase Prp28 was identified as a potential mediator of this switch, an event essential for catalysis of splicing.
35. Kuhn A.N., Li Z., Brow D.A. Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome. Mol Cell. 3:1999;65-75. A mutation in U4 was identified that blocks the unwinding of the U4/U6 duplex and the activation of the spliceosome. A specific mutation in the U5 snRNP protein Prp8 suppresses the U4 mutation, indicating a key role for Prp8 in activating the spliceosome for catalysis.
36. Gottschalk A., Neubauer G., Banroques J., Mann M., Luhrmann R., Fabrizio P. Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP. EMBO J. 18:1999;4535-4548.
37. Stevens S.W., Abelson J. Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins. Proc Natl Acad Sci USA. 96:1999;7226-7231.
38. Luo H.R., Moreau G.A., Levin N., Moore M.J. The human Prp8 protein is a component of both U2- and U12-dependent spliceosomes. RNA. 5:1999;893-908.
39. Umen J.G., Guthrie C. The second catalytic step of pre-mRNA splicing. RNA. 1:1995;869-885.
40. 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. 13:1999;1970-1982. A tertiary interaction between U6 snRNA and the 5′ and 3′ splice sites involves Prp8, suggesting that Prp8 may be at the catalytic center of the spliceosome.
41. Siatecka M., Reyes J.L., Konarska M.M. Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center. Genes Dev. 13:1999;1983-1993. A specific region of Prp8 was identified that interacts genetically with both 5′ and 3′ splice sites. Together with RNA-protein interaction studies, the data suggest that Prp8 is at the catalytic center of the spliceosome.
42. Chua K., Reed R. Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing. Genes Dev. 13:1999;841-850.
43. Chua K., Reed R. The RNA splicing factor hSlu7 is required for correct 3′ splice site choice. Nature. 402:1999;207-211. hSlu7 was found to be required for holding exon 1 properly in the spliceosome and for selection of a pre-specified AG during catalytic step II of splicing.
44. Segault V., Will C.L., Polycarpou-Schwarz M., Mattaj I.W., Branlant C., Luhrmann R. Conserved loop I of U5 small nuclear RNA is dispensable for both catalytic steps of pre-mRNA splicing in HeLa nuclear extracts. Mol Cell Biol. 19:1999;2782-2790.