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Article

Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling.

Nature communications - 25 May 2021

Yeh Fu-Lung, Chang Shang-Lin, Ahmed Golam Rizvee, Liu Hsin-I, Tung Luh, Yeh Chung-Shu, Lanier Leah Stands, Maeder Corina, Lin Che-Min, Tsai Shu-Chun, Hsiao Wan-Yi, Chang Wei-Hau, Chang Tien-Hsien

Abstract excerpt

Splicing, a key step in the eukaryotic gene-expression pathway, converts precursor messenger RNA (pre-mRNA) into mRNA by excising introns and ligating exons. This task is accomplished by the spliceosome, a macromolecular machine that must undergo sequential conformational changes to establish its active site. Each of these major changes requires a dedicated DExD/H-box ATPase, but how these enzymes are activated...

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Identifiers

PMID: 34035302
DOI: 10.1038/s41467-021-23459-4
PMCID: PMC8149812

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling.PMID 34035302Read ↗

Structural elucidation of a PRP8 core domain from the heart of the spliceosome.Semantic proximity Read ↗

The DExD/H-box ATPase Prp2p destabilizes and proofreads the catalytic RNA core of the spliceosome.Semantic proximity Read ↗

A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity.Semantic proximity Read ↗

Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation.Semantic proximity Read ↗

Allele-specific genetic interactions between Prp8 and RNA active site residues suggest a function for Prp8 at the catalytic core of the spliceosome.Semantic proximity Read ↗

Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly.Semantic proximity Read ↗

A composite double-/single-stranded RNA-binding region in protein Prp3 supports tri-snRNP stability and splicing.Semantic proximity Read ↗

ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8.Semantic proximity Read ↗

Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site.Semantic proximity Read ↗

Opposing classes of prp8 alleles modulate the transition between the catalytic steps of pre-mRNA splicing.Semantic proximity Read ↗

Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones.Semantic proximity Read ↗

Crystal structure of Prp5p reveals interdomain interactions that impact spliceosome assembly.Semantic proximity Read ↗

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