Splicing factor SF1 from Drosophila and Caenorhabditis: presence of an N-terminal RS domain and requirement for viability
- PMID: 10606272
- PMCID: PMC1369883
- DOI: 10.1017/s1355838299991872
Splicing factor SF1 from Drosophila and Caenorhabditis: presence of an N-terminal RS domain and requirement for viability
Abstract
Splicing factor SF1 contributes to the recognition of the 3' splice site by interacting with U2AF65 and binding to the intron branch site during the formation of the early splicing complex E. These interactions and the essential functional domains of SF1 are highly conserved in Saccharomyces cerevisiae. We have isolated cDNAs encoding SF1 from Drosophila (Dm) and Caenorhabditis (Ce). The encoded proteins share the U2AF65 interaction domain, a hnRNP K homology domain, and one or two zinc knuckles required for RNA binding as well as Pro-rich C-terminal sequences with their yeast and mammalian counterparts. In contrast to SF1 in other species, DmSF1 and CeSF1 are characterized by an N-terminal region enriched in Ser, Arg, Lys, and Asp residues with homology to the RS domains of several splicing proteins. These domains mediate protein-protein or protein-RNA interactions, suggesting an additional role for DmSF1 and CeSF1 in pre-mRNA splicing. Human (Hs), fly, and worm SF1 interact equally well with HsU2AF65 or the Drosophila homolog DmU2AF50. Moreover, DmSF1 lacking its N terminus is functional in prespliceosome formation in a HeLa splicing system, emphasizing the conserved nature of interactions at an early step in spliceosome assembly. The Ce-SF1 gene is located in a polycistronic transcription unit downstream of the genes encoding U2AF35 (uaf-2) and a cyclophilin (cyp-13), implying the coordinate transcriptional regulation of these genes. Injection of double-stranded RNA into C. elegans results in embryonic lethality; thus, the SF1 gene is essential not only in yeast but also in at least one metazoan.
Similar articles
-
Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomyces cerevisiae pre-mRNA splicing factor SF1.RNA. 1998 May;4(5):551-65. doi: 10.1017/s1355838298980335. RNA. 1998. PMID: 9582097 Free PMC article.
-
Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA.RNA. 1996 Aug;2(8):794-810. RNA. 1996. PMID: 8752089 Free PMC article.
-
Recognition of RNA branch point sequences by the KH domain of splicing factor 1 (mammalian branch point binding protein) in a splicing factor complex.Mol Cell Biol. 2001 Aug;21(15):5232-41. doi: 10.1128/MCB.21.15.5232-5241.2001. Mol Cell Biol. 2001. PMID: 11438677 Free PMC article.
-
The branchpoint binding protein: in and out of the spliceosome cycle.Adv Exp Med Biol. 2010;693:123-41. Adv Exp Med Biol. 2010. PMID: 21189690 Review.
-
STAR, a gene family involved in signal transduction and activation of RNA.Trends Genet. 1997 Dec;13(12):479-84. doi: 10.1016/s0168-9525(97)01269-9. Trends Genet. 1997. PMID: 9433137 Review.
Cited by
-
Mutations in the Caenorhabditis elegans U2AF large subunit UAF-1 alter the choice of a 3' splice site in vivo.PLoS Genet. 2009 Nov;5(11):e1000708. doi: 10.1371/journal.pgen.1000708. Epub 2009 Nov 6. PLoS Genet. 2009. PMID: 19893607 Free PMC article.
-
Pre-spliceosome formation in S.pombe requires a stable complex of SF1-U2AF(59)-U2AF(23).EMBO J. 2002 Oct 15;21(20):5516-26. doi: 10.1093/emboj/cdf555. EMBO J. 2002. PMID: 12374752 Free PMC article.
-
A dual role for BBP/ScSF1 in nuclear pre-mRNA retention and splicing.EMBO J. 2000 Apr 17;19(8):1873-86. doi: 10.1093/emboj/19.8.1873. EMBO J. 2000. PMID: 10775271 Free PMC article.
-
Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.Nucleic Acids Res. 2015 Dec 2;43(21):10456-73. doi: 10.1093/nar/gkv952. Epub 2015 Sep 29. Nucleic Acids Res. 2015. PMID: 26420826 Free PMC article.
-
SPLICING FACTOR1 Is Important in Chloroplast Development under Cold Stress.Plant Physiol. 2020 Oct;184(2):973-987. doi: 10.1104/pp.20.00706. Epub 2020 Jul 30. Plant Physiol. 2020. PMID: 32732348 Free PMC article.
References
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Molecular Biology Databases