Prp43p is a DEAH-box spliceosome disassembly factor essential for ribosome biogenesis.
Mol Cell Biol, 2006/1;26(2):523-34.
Combs DJ[1], Nagel RJ, Ares M Jr, Stevens SW
Affiliations
PMID: 16382144
Impact factor: 5.069
Abstract
The known function of the DEXH/D-box protein Prp43p is the removal of the U2, U5, and U6 snRNPs from the postsplicing lariat-intron ribonucleoprotein complex. We demonstrate that affinity-purified Prp43p-associated material includes the expected spliceosomal components; however, we also identify several preribosomal complexes that are specifically purified with Prp43p. Conditional prp43 mutant alleles confer a 35S pre-rRNA processing defect, with subsequent depletion of 27S and 20S precursors. Upon a shift to a nonpermissive temperature, both large and small-ribosomal-subunit proteins accumulate in the nucleolus of prp43 mutants. Pulse-chase analysis demonstrates delayed kinetics of 35S, 27S, and 20S pre-rRNA processing with turnover of these intermediates. Microarray analysis of pre-mRNA splicing defects in prp43 mutants shows a very mild effect, similar to that of nonessential pre-mRNA splicing factors. Prp43p is the first DEXH/D-box protein shown to function in both RNA polymerase I and polymerase II transcript metabolism. Its essential function is in its newly characterized role in ribosome biogenesis of both ribosomal subunits, positioning Prp43p to regulate both pre-mRNA splicing and ribosome biogenesis.
MeSH terms
Cell Nucleolus; Computational Biology; DEAD-box RNA Helicases; Introns; Mutation; Oligonucleotide Array Sequence Analysis; RNA Helicases; RNA Polymerase I; RNA Polymerase II; RNA Precursors; RNA Splicing; RNA, Small Nuclear; Ribosomes; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
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