期刊
FEBS LETTERS
卷 597, 期 3, 页码 448-457出版社
WILEY
DOI: 10.1002/1873-3468.14555
关键词
outron-containing transcripts; pre-mRNA splicing; spliceosome; trans-splicing and C; elegans
UBL-5 is a ubiquitin-like protein that associates with proteins non-covalently and plays a conserved pre-mRNA splicing function in Caenorhabditis elegans. UBL-5 interacts with splicing factors Snu66/SART-1 and PRP-38 and other spliceosomal proteins. UBL-5 mutants in C. elegans exhibit developmental defects and splicing abnormalities for specific targets.
The ubiquitin-like protein Hub1/UBL-5 associates with proteins non-covalently. Hub1 promotes alternative splicing and splicing of precursor mRNAs with weak introns in yeast and mammalian cells; however, its splicing function has remained elusive in multicellular organisms. Here, we demonstrate the splicing function of Hub1/UBL-5 in the free-living nematode Caenorhabditis elegans. Hub1/UBL-5 binds to the HIND-containing splicing factors Snu66/SART-1 and PRP-38 and associates with other spliceosomal proteins. C. elegans hub1/ubl-5 mutants die at the Larval 3 stage and show splicing defects for selected targets, similar to the mutants in yeast and mammalian cells. UBL-5 complemented growth and splicing defects in Schizosaccharomyces pombe hub1 mutants, confirming its functional conservation. Thus, UBL-5 is important for C. elegans development and plays a conserved pre-mRNA splicing function.
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