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Related Experiment Video

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ACT1-CUP1 Assays Determine the Substrate-Specific Sensitivities of Spliceosomal Mutants in Budding Yeast

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Mechanism for Aar2p function as a U5 snRNP assembly factor.

Gert Weber¹, Vanessa F Cristão, Flavia de L Alves

¹Fachbereich Biologie/Chemie/Pharmazie, Abteilung Strukturbiochemie, Freie Universität Berlin, D-14195 Berlin, Germany;

Genes & Development

|July 19, 2011

Summary

This summary is machine-generated.

Aar2 protein regulates the assembly of Brr2p, a crucial RNA helicase, onto U5 small nuclear ribonucleoproteins (snRNPs). Phosphorylation of Aar2p controls its interaction with Prp8p, facilitating Brr2p incorporation for proper spliceosome function.

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Published on: June 30, 2022

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

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Published on: August 9, 2019

Area of Science:

Molecular Biology
RNA Biology
Protein Biochemistry

Background:

Assembly of particle-specific proteins onto spliceosomal small nuclear ribonucleoproteins (snRNPs) is not well understood.
Brr2p is a U5 snRNP-specific RNA helicase essential for spliceosome activation and disassembly.

Purpose of the Study:

To investigate the mechanism by which Aar2p regulates the incorporation of Brr2p into U5 snRNPs.
To elucidate the role of Aar2p as a potential U5 snRNP assembly factor.

Main Methods:

Co-immunoprecipitation assays to study protein-protein interactions.
Analysis of yeast strains with specific mutations (e.g., phospho-mimetic mutation S253E in Aar2p).
In vivo phosphorylation studies of Aar2p.

Main Results:

Aar2p and Brr2p bind to distinct domains in Prp8p: Aar2p to the RNaseH domain and Brr2p to the Jab1/MPN domain.
The Aar2p-Prp8p complex prevents Brr2p binding by sequestering the Jab1/MPN domain.
Phosphorylation of Aar2p disrupts the Aar2p-Prp8p interaction, favoring Brr2p binding.

Conclusions:

Aar2p functions as a phosphorylation-regulated assembly factor for U5 snRNPs.
Phosphorylation controls the switch between Aar2p and Brr2p binding to Prp8p, regulating Brr2p incorporation.
This regulation may prevent non-specific RNA binding and premature Brr2p activation.