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Article

A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing.

Cell - 9 Mar 1990

Burgess S, Couto J R, Guthrie C

Abstract excerpt

We previously described a dominant suppressor of the splicing defect conferred by an A----C intron branchpoint mutation in S. cerevisiae. Suppression occurs by increasing the frequency with which the mutant branchpoint is utilized. We have now cloned the genomic region encoding the prp16-1 suppressor function and have demonstrated that PRP16 is essential for viability. A 1071 amino acid open reading frame...

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PMID: 2138057
DOI: 10.1016/0092-8674(90)90086-t

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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A putative ATP binding protein influences the fidelity of branchpoint recognition in yeast splicing.PMID 2138057Read ↗

A dominant negative mutation in a spliceosomal ATPase affects ATP hydrolysis but not binding to the spliceosome.Semantic proximity Read ↗

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The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing.Semantic proximity Read ↗

Characterization of Cwc2, U6 snRNA, and Prp8 interactions destabilized by Prp16 ATPase at the transition between the first and second steps of splicing.Semantic proximity Read ↗

Genetic interactions between the yeast RNA helicase homolog Prp16 and spliceosomal snRNAs identify candidate ligands for the Prp16 RNA-dependent ATPase.Semantic proximity Read ↗

The DEAH-box splicing factor Prp16 unwinds RNA duplexes in vitro.Semantic proximity Read ↗

Control of 3' splice site selection in S. cerevisiae by a highly conserved amino acid within the Prp8 α-finger domain.Semantic proximity Read ↗

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