The yeast Prp3 protein is a U4/U6 snRNP protein necessary for integrity of the U4/U6 snRNP and the U4/U6.U5 tri-snRNP - PubMed
The yeast Prp3 protein is a U4/U6 snRNP protein necessary for integrity of the U4/U6 snRNP and the U4/U6.U5 tri-snRNP
J G Anthony et al. RNA. 1997 Oct.
Abstract
Previously, yeast prp3 mutants were found to be blocked prior to the first catalytic step of pre-mRNA splicing. No splicing intermediates or products are formed from pre-mRNA in heat-inactivated prp3 mutants or prp3 mutant extracts. Here we show that Prp3p is a component of the U4/U6 snRNP and is also present in the U4/U6.U5 tri-snRNP. Heat inactivation of prp3 extracts results in depletion of free U6 snRNPs and U4/U6.U5 tri-snRNPs, but not U4/U6 snRNPs or U5 snRNPs. Free U4 snRNP, normally not present in wild-type extracts, accumulates under these conditions. Assays of in vivo levels of snRNAs in a prp3 mutant revealed that amounts of free U6 snRNA decreased, free U4 snRNA increased, and U4/U6 hybrids decreased slightly. These results suggest that Prp3p is required for formation of stable U4/U6 snRNPs and for assembly of the U4/U6.U5 tri-snRNP from its component snRNPs. Upon inactivation of Prp3p, spliceosomes cannot assemble from prespliceosomes due to the absence of intact U4/U6.U5 tri-snRNPs. Prp3p is homologous to a human protein that is a component of U4/U6 snRNPs, exemplifying the conservation of splicing factors between yeast and metazoans.
Similar articles
-
Galisson F, Legrain P. Galisson F, et al. Nucleic Acids Res. 1993 Apr 11;21(7):1555-62. doi: 10.1093/nar/21.7.1555. Nucleic Acids Res. 1993. PMID: 8479905 Free PMC article.
-
Liu S, Mozaffari-Jovin S, Wollenhaupt J, Santos KF, Theuser M, Dunin-Horkawicz S, Fabrizio P, Bujnicki JM, Lührmann R, Wahl MC. Liu S, et al. Elife. 2015 Jul 10;4:e07320. doi: 10.7554/eLife.07320. Elife. 2015. PMID: 26161500 Free PMC article.
-
Makarova OV, Makarov EM, Liu S, Vornlocher HP, Lührmann R. Makarova OV, et al. EMBO J. 2002 Mar 1;21(5):1148-57. doi: 10.1093/emboj/21.5.1148. EMBO J. 2002. PMID: 11867543 Free PMC article.
-
CryoEM structures of two spliceosomal complexes: starter and dessert at the spliceosome feast.
Nguyen TH, Galej WP, Fica SM, Lin PC, Newman AJ, Nagai K. Nguyen TH, et al. Curr Opin Struct Biol. 2016 Feb;36:48-57. doi: 10.1016/j.sbi.2015.12.005. Epub 2016 Jan 21. Curr Opin Struct Biol. 2016. PMID: 26803803 Free PMC article. Review.
-
Pre-mRNA splicing: the discovery of a new spliceosome doubles the challenge.
Tarn WY, Steitz JA. Tarn WY, et al. Trends Biochem Sci. 1997 Apr;22(4):132-7. doi: 10.1016/s0968-0004(97)01018-9. Trends Biochem Sci. 1997. PMID: 9149533 Review.
Cited by
-
MRN1 implicates chromatin remodeling complexes and architectural factors in mRNA maturation.
Düring L, Thorsen M, Petersen DS, Køster B, Jensen TH, Holmberg S. Düring L, et al. PLoS One. 2012;7(9):e44373. doi: 10.1371/journal.pone.0044373. Epub 2012 Sep 18. PLoS One. 2012. PMID: 23028530 Free PMC article.
-
PRPF31-retinitis pigmentosa: Challenges and opportunities for clinical translation.
Aweidah H, Xi Z, Sahel JA, Byrne LC. Aweidah H, et al. Vision Res. 2023 Dec;213:108315. doi: 10.1016/j.visres.2023.108315. Epub 2023 Sep 14. Vision Res. 2023. PMID: 37714045 Free PMC article. Review.
-
Chen X, Luan X, Zheng Q, Qiao C, Chen W, Wang M, Yan Y, Xie B, Shen C, He Z, Zhang J, Liu M, Hu X, Li H, Zheng B, Fang J, Yu J. Chen X, et al. Sci Rep. 2019 Jul 10;9(1):9988. doi: 10.1038/s41598-019-46419-x. Sci Rep. 2019. PMID: 31292463 Free PMC article.
-
SUMO conjugation to spliceosomal proteins is required for efficient pre-mRNA splicing.
Pozzi B, Bragado L, Will CL, Mammi P, Risso G, Urlaub H, Lührmann R, Srebrow A. Pozzi B, et al. Nucleic Acids Res. 2017 Jun 20;45(11):6729-6745. doi: 10.1093/nar/gkx213. Nucleic Acids Res. 2017. PMID: 28379520 Free PMC article.
-
Lee BH, Kapoor A, Zhu J, Zhu JK. Lee BH, et al. Plant Cell. 2006 Jul;18(7):1736-49. doi: 10.1105/tpc.106.042184. Epub 2006 Jun 2. Plant Cell. 2006. PMID: 16751345 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases