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RNA helicase dynamics in pre-mRNA splicing.

TitleRNA helicase dynamics in pre-mRNA splicing.
Publication TypeJournal Article
Year of Publication2000
AuthorsSchwer B, Meszaros T
JournalEMBO J
Volume19
Issue23
Pagination6582-91
Date Published2000 Dec 1
ISSN0261-4189
KeywordsAcid Anhydride Hydrolases, Adenosine Triphosphate, Amino Acid Sequence, Catalysis, Cell Division, DEAD-box RNA Helicases, Dose-Response Relationship, Drug, Fungal Proteins, Genes, Dominant, Hydrolysis, Isoleucine, Molecular Sequence Data, Mutation, Missense, Nucleoside-Triphosphatase, Phenotype, Plasmids, Protein Structure, Tertiary, Recombinant Proteins, RNA Helicases, RNA Splicing, RNA, Double-Stranded, RNA, Messenger, Saccharomyces cerevisiae Proteins, Spliceosomes, Suppression, Genetic, Temperature, Valine, Yeasts
Abstract

The DExH-box NTPase/helicase Prp22p plays two important roles in pre-mRNA splicing. It promotes the second transesterification reaction and then catalyzes the ATP-dependent release of mature mRNA from the spliceosome. Evidence that helicase activity is important emerged from the analysis of Prp22p motif III (SAT) mutations that uncouple the NTPase and helicase activities. We find that S635A and T637A hydrolyse ATP, but are defective in unwinding duplex RNA and releasing mRNA from the spliceosome. The S635A mutation is lethal in vivo at

DOI10.1093/emboj/19.23.6582
Alternate JournalEMBO J.
PubMed ID11101530
PubMed Central IDPMC305851
Grant ListGM50288 / GM / NIGMS NIH HHS / United States

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