Submitted by mam2155 on March 24, 2014 - 4:20pm
| Title | RNA helicase dynamics in pre-mRNA splicing. |
| Publication Type | Journal Article |
| Year of Publication | 2000 |
| Authors | Schwer B, Meszaros T |
| Journal | EMBO J |
| Volume | 19 |
| Issue | 23 |
| Pagination | 6582-91 |
| Date Published | 2000 Dec 1 |
| ISSN | 0261-4189 |
| Keywords | Acid 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 |
| DOI | 10.1093/emboj/19.23.6582 |
| Alternate Journal | EMBO J. |
| PubMed ID | 11101530 |
| PubMed Central ID | PMC305851 |
| Grant List | GM50288 / GM / NIGMS NIH HHS / United States |