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• W3011201428 endingPage "7170" @default.
• W3011201428 startingPage "7159" @default.
• W3011201428 abstract "RNA helicases of the DEAH/RHA family are involved in many essential cellular processes, such as splicing or ribosome biogenesis, where they remodel large RNA–protein complexes to facilitate transitions to the next intermediate. DEAH helicases couple adenosine triphosphate (ATP) hydrolysis to conformational changes of their catalytic core. This movement results in translocation along RNA, which is held in place by auxiliary C-terminal domains. The activity of DEAH proteins is strongly enhanced by the large and diverse class of G-patch activators. Despite their central roles in RNA metabolism, insight into the molecular basis of G-patch–mediated helicase activation is missing. Here, we have solved the structure of human helicase DHX15/Prp43, which has a dual role in splicing and ribosome assembly, in complex with the G-patch motif of the ribosome biogenesis factor NKRF. The G-patch motif binds in an extended conformation across the helicase surface. It tethers the catalytic core to the flexibly attached C-terminal domains, thereby fixing a conformation that is compatible with RNA binding. Structures in the presence or absence of adenosine diphosphate (ADP) suggest that motions of the catalytic core, which are required for ATP binding, are still permitted. Concomitantly, RNA affinity, helicase, and ATPase activity of DHX15 are increased when G-patch is bound. Mutations that detach one end of the tether but maintain overall binding severely impair this enhancement. Collectively, our data suggest that the G-patch motif acts like a flexible brace between dynamic portions of DHX15 that restricts excessive domain motions but maintains sufficient flexibility for catalysis." @default.
• W3011201428 created "2020-03-23" @default.
• W3011201428 creator A5019580976 @default.
• W3011201428 creator A5049744007 @default.
• W3011201428 creator A5055603134 @default.
• W3011201428 creator A5067633818 @default.
• W3011201428 creator A5089720531 @default.
• W3011201428 date "2020-03-16" @default.
• W3011201428 modified "2023-10-16" @default.
• W3011201428 title "Structural basis for DEAH-helicase activation by G-patch proteins" @default.
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• W3011201428 doi "https://doi.org/10.1073/pnas.1913880117" @default.
• W3011201428 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7132122" @default.
• W3011201428 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32179686" @default.
• W3011201428 hasPublicationYear "2020" @default.
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