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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Spliceosomes

 
 
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Disease relevance of Spliceosomes

 

High impact information on Spliceosomes

  • As a key regulatory step in this signaling pathway, the mRNA encoding the UPR-specific transcription factor Hac1p becomes spliced by a unique mechanism that requires tRNA ligase but not the spliceosome [3].
  • Our results suggest that the regulated splicing of HAC1 mRNA occurs by a novel pathway, involving tRNA ligase and bypassing the spliceosome [4].
  • Analysis of the requirements of these interactions demonstrates that the 5'SS RNA is recognized independently by at least two different elements during spliceosome assembly: the 5' end of U1 snRNA and a component(s) of the U2-U4-U5-U6 snRNP complex [5].
  • The peptide acts at a step in the assembly of splicing complexes, suggesting that one of the functions of the basic region of Rev is to prevent formation of a functional spliceosome [6].
  • We propose that PRP16 is an excellent candidate for mediating one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis [7].
 

Biological context of Spliceosomes

 

Anatomical context of Spliceosomes

 

Associations of Spliceosomes with chemical compounds

  • With Mg2+, U6 snRNA with a sulphur substitution for the pro-Rp or pro-Sp non-bridging phosphoryl oxygen of nucleotide U80 reconstitutes a fully assembled yet catalytically inactive spliceosome [17].
  • The 4F4 antibody does not prevent the adenosine triphosphate-dependent formation of a 60S splicing complex (spliceosome) [18].
  • To probe their interactions within the active center of the mammalian spliceosome, substrates containing a single photoactivatable 4-thiouridine residue adjacent to either splice site were synthesized, and crosslinks were induced during the course of in vitro splicing [19].
  • Thus, mutations in the mammalian BPS appear to uncouple spliceosome assembly from cleavage at the 5' splice site and lariat formation [20].
  • Glycerol gradient fractionation showed that a subset of these proteins remain associated with mRNA after its release from the spliceosome [21].
 

Gene context of Spliceosomes

  • Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes [22].
  • This was unexpected because previous analysis has demonstrated that the U5 snRNP protein encoded by PRP8 is required for spliceosome assembly prior to the first catalytic step of splicing [23].
  • The experiments identify a specific inter-snRNP protein-protein contact that occurs during spliceosome assembly and more generally support substantial functional similarity between U2AF65 and MUD2P [24].
  • We isolated by glycerol gradient sedimentation spliceosomes that were formed in yeast extracts depleted of PRP16 [25].
  • These observations likely reflect the function of the SRPK family of kinases in spliceosome assembly and in mediating the trafficking of splicing factors in mammalian cells [26].
 

Analytical, diagnostic and therapeutic context of Spliceosomes

  • Thus, the efficiency of splicing at the env 3' splice site can be affected at the level of spliceosome assembly, lariat formation, or cleavage at the 3' splice site and exon ligation [27].
  • To investigate the mechanism of spliceosome assembly in vivo, we performed chromatin immunoprecipitation (ChIP) analysis of U1, U2, and U5 small nuclear ribonucleoprotein particles (snRNPs) to intron-containing yeast (S. cerevisiae) genes [28].
  • Immunoprecipitation with anti-PRP2 antibodies confirmed that dominant negative PRP2 protein competed with its wild-type counterpart for interaction with spliceosomes, with which the mutant protein remained associated [29].
  • This result, combined with a comparison of the structure with known RRMs and pseudoRRMs as well as model-building by using the electron cryomicroscopy structure of a spliceosomal U11/U12 di-snRNP, suggests that p14.SF3b155 presents a noncanonical surface for RNA recognition at the heart of the mammalian spliceosome [30].
  • In situ hybridizations reveal that centrin, cyclin B, and beta-tubulin mRNAs are present in both sterile and spermatogenous cells, but that transcripts encoding RNA helicase and PRP-19 (a spliceosome component) become localized in spermatogenous cells [31].

References

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  2. Imprinted genes in the Prader-Willi deletion. Francke, U. Novartis Found. Symp. (1998) [Pubmed]
  3. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Sidrauski, C., Walter, P. Cell (1997) [Pubmed]
  4. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Sidrauski, C., Cox, J.S., Walter, P. Cell (1996) [Pubmed]
  5. Disruption of base pairing between the 5' splice site and the 5' end of U1 snRNA is required for spliceosome assembly. Konforti, B.B., Koziolkiewicz, M.J., Konarska, M.M. Cell (1993) [Pubmed]
  6. Specific regulation of mRNA splicing in vitro by a peptide from HIV-1 Rev. Kjems, J., Frankel, A.D., Sharp, P.A. Cell (1991) [Pubmed]
  7. A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing. Burgess, S., Couto, J.R., Guthrie, C. Cell (1990) [Pubmed]
  8. Genetic evidence for base pairing between U2 and U6 snRNA in mammalian mRNA splicing. Datta, B., Weiner, A.M. Nature (1991) [Pubmed]
  9. Messenger RNA splicing in yeast: clues to why the spliceosome is a ribonucleoprotein. Guthrie, C. Science (1991) [Pubmed]
  10. Correspondence between a mammalian spliceosome component and an essential yeast splicing factor. Bennett, M., Reed, R. Science (1993) [Pubmed]
  11. Cotranscriptional spliceosome assembly occurs in a stepwise fashion and requires the cap binding complex. Görnemann, J., Kotovic, K.M., Hujer, K., Neugebauer, K.M. Mol. Cell (2005) [Pubmed]
  12. SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Rappsilber, J., Ajuh, P., Lamond, A.I., Mann, M. J. Biol. Chem. (2001) [Pubmed]
  13. Coiled bodies in the nucleolus of breast cancer cells. Ochs, R.L., Stein, T.W., Tan, E.M. J. Cell. Sci. (1994) [Pubmed]
  14. NS1-Binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells. Wolff, T., O'Neill, R.E., Palese, P. J. Virol. (1998) [Pubmed]
  15. An exonic splicing enhancer in human IGF-I pre-mRNA mediates recognition of alternative exon 5 by the serine-arginine protein splicing factor-2/alternative splicing factor. Smith, P.J., Spurrell, E.L., Coakley, J., Hinds, C.J., Ross, R.J., Krainer, A.R., Chew, S.L. Endocrinology (2002) [Pubmed]
  16. The immunolocalization of small nuclear ribonucleoprotein particles in testicular cells during the cycle of the seminiferous epithelium of the adult rat. Moussa, F., Oko, R., Hermo, L. Cell Tissue Res. (1994) [Pubmed]
  17. Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome. Yean, S.L., Wuenschell, G., Termini, J., Lin, R.J. Nature (2000) [Pubmed]
  18. Heterogeneous nuclear ribonucleoproteins: role in RNA splicing. Choi, Y.D., Grabowski, P.J., Sharp, P.A., Dreyfuss, G. Science (1986) [Pubmed]
  19. The U5 and U6 small nuclear RNAs as active site components of the spliceosome. Sontheimer, E.J., Steitz, J.A. Science (1993) [Pubmed]
  20. The role of the mammalian branchpoint sequence in pre-mRNA splicing. Reed, R., Maniatis, T. Genes Dev. (1988) [Pubmed]
  21. Pre-mRNA splicing alters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Le Hir, H., Moore, M.J., Maquat, L.E. Genes Dev. (2000) [Pubmed]
  22. Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Company, M., Arenas, J., Abelson, J. Nature (1991) [Pubmed]
  23. A novel role for a U5 snRNP protein in 3' splice site selection. Umen, J.G., Guthrie, C. Genes Dev. (1995) [Pubmed]
  24. The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Abovich, N., Liao, X.C., Rosbash, M. Genes Dev. (1994) [Pubmed]
  25. SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing. Ansari, A., Schwer, B. EMBO J. (1995) [Pubmed]
  26. SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. Wang, H.Y., Lin, W., Dyck, J.A., Yeakley, J.M., Songyang, Z., Cantley, L.C., Fu, X.D. J. Cell Biol. (1998) [Pubmed]
  27. The role of branchpoint and 3'-exon sequences in the control of balanced splicing of avian retrovirus RNA. Fu, X.D., Katz, R.A., Skalka, A.M., Maniatis, T. Genes Dev. (1991) [Pubmed]
  28. Cotranscriptional spliceosome assembly dynamics and the role of U1 snRNA:5'ss base pairing in yeast. Lacadie, S.A., Rosbash, M. Mol. Cell (2005) [Pubmed]
  29. A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes. Plumpton, M., McGarvey, M., Beggs, J.D. EMBO J. (1994) [Pubmed]
  30. Crystal structure of a core spliceosomal protein interface. Schellenberg, M.J., Edwards, R.A., Ritchie, D.B., Kent, O.A., Golas, M.M., Stark, H., Lührmann, R., Glover, J.N., MacMillan, A.M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  31. Differential segregation and modification of mRNA during spermiogenesis in Marsilea vestita. Tsai, C.W., Van Der Weele, C.M., Wolniak, S.M. Dev. Biol. (2004) [Pubmed]
 
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