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DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling

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Published on: October 8, 2019

U2AF⁶⁵ assemblies drive sequence-specific splice site recognition.

Manel Tari¹, Valérie Manceau², Jean de Matha Salone¹

¹SABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, Evry, France.

|July 5, 2019

Summary

The splicing factors U2AF⁶⁵ and CAPERα cooperatively bind SF3b155, forming RNA-driven liquid assemblies. These assemblies regulate exon skipping, impacting alternative splicing and gene expression.

Keywords:

RBM39 SF3b1 U2AF2 liquid-liquid phase separation splicing

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Area of Science:

Molecular Biology
RNA Biology
Gene Regulation

Background:

U2AF⁶⁵ is crucial for splicing, anchoring U2 snRNP via its UHM domain interacting with SF3b155.
SF3b155 is a key U2 snRNP protein with a multi-ULM domain.

Purpose of the Study:

To investigate the cooperative binding of U2AF⁶⁵ and CAPERα to SF3b155.
To explore the role of U2AF⁶⁵'s RS domain in phase separation and its regulation by RNA.
To determine the cellular impact of U2AF⁶⁵ and CAPERα on alternative splicing.

Main Methods:

Cooperative binding assays to study protein interactions.
Liquid-liquid phase separation experiments.
RNA binding studies with pyrimidine-rich sequences.
Cellular knockdown experiments to assess splicing changes.

Main Results:

U2AF⁶⁵ and CAPERα bind cooperatively to SF3b155's multi-ULM domain.
U2AF⁶⁵'s RS domain drives RNA-dependent liquid-liquid phase separation.
Knockdown of U2AF⁶⁵ or CAPERα enhances cassette exon inclusion preceded by pyrimidine-rich motifs.
These findings support a model of RNA-guided condensate formation regulating splicing.

Conclusions:

Dynamic condensates of U2AF⁶⁵ and CAPERα on repetitive RNA influence splice site choice.
Posttranslational modifications and recruited proteins may further refine splicing regulation within these condensates.
This study sheds light on the mechanisms of alternative splicing and gene expression control.