ArticleBiochemistry2006
Mutations in PRP43 that uncouple RNA-dependent NTPase activity and pre-mRNA splicing function.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 76 citations in OpenAlex.
- Conserved motifs in the flavivirus NS3 RNA helicase enzyme.Wiley interdisciplinary reviews. RNA · 2022Review
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
- DEAH-Box RNA Helicases in Pre-mRNA Splicing.Trends in biochemical sciences · 2021Review
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- Auxiliary domains of the HrpB bacterial DExH-box helicase shape its RNA preferences.RNA biology · 2020Article
- Structural basis for DEAH-helicase activation by G-patch proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Function of Auxiliary Domains of the DEAH/RHA Helicase DHX36 in RNA Remodeling.Journal of molecular biology · 2020Article
- Termination of pre-mRNA splicing requires that the ATPase and RNA unwindase Prp43p acts on the catalytic snRNA U6.Genes & development · 2019Article
- Early splicing functions of fission yeast Prp16 and its unexpected requirement for gene Silencing is governed by intronic features.RNA biology · 2019Article
- Structural basis for RNA translocation by DEAH-box ATPases.Nucleic acids research · 2019Article
- Structures of the human spliceosomes before and after release of the ligated exon.Cell research · 2019Article
- Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs.Biochemical Society transactions · 2017Review
- Identification of a 35S U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-snRNP) complex intermediate in spliceosome assembly.The Journal of biological chemistry · 2017Article
- De Novo Missense Mutations in DHX30 Impair Global Translation and Cause a Neurodevelopmental Disorder.American journal of human genetics · 2017Article
- Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.RNA (New York, N.Y.) · 2017Article
- The crystal structure of human DEAH-box RNA helicase 15 reveals a domain organization of the mammalian DEAH/RHA family.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Regulation of Prp43-mediated disassembly of spliceosomes by its cofactors Ntr1 and Ntr2.Nucleic acids research · 2017Article
- Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.Nucleic acids research · 2017Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Saccharomyces cerevisiae Prp43 is a DEAH-box RNA-dependent ATPase that catalyzes the release of excised lariat intron from the mRNA spliceosome. Previous studies identified mutations in Prp43 motifs I, II, and VI that were lethal in vivo and ablated ATP hydrolysis in vitro. Such Prp43 mutants exerted dominant-negative growth phenotypes when expressed in wild type cells and blocked intron release in vitro when added to yeast splicing extracts. Here, we assessed the effects of alanine and conservative substitutions at conserved residues in motifs Ia ((146)TQPRRVAA(153)), IV ((307)LLFLTG(312)), and V ((376)TNIAETSLT(384)) and thereby identified Arg150 (motif Ia), Phe309 (motif IV), Thr376, Leu383, and Thr384 (motif V) as being important for Prp43 function in vivo. Motif V mutations T376V, T384A, and T384V were lethal and dominant negative in vivo, and the mutant proteins inhibited lariat release in vitro. The T384A and T384V proteins were proficient for ATP hydrolysis, suggesting that ATPase activity is necessary, but not sufficient, for Prp43 function. We report that Prp43 hydrolyzes all common NTPs and dNTPs and unwinds short 5'/3' tailed RNA/DNA duplexes in an ATP-dependent fashion. Optimal ATP hydrolysis requires an RNA cofactor of >or=20 nt. Prp43 is largely indifferent to mutations in its C-terminal segment, which is conserved in the DEAH-box splicing factors Prp2, Prp16, and Prp22.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.