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Splicing at the phase-separated nuclear speckle interface: a model.

Susan E Liao¹, Oded Regev¹

¹Computer Science Department, Courant Institute of Mathematical Sciences, New York University, New York, NY, USA.

Nucleic Acids Research

|December 18, 2020

Summary

This summary is machine-generated.

Phase-separated membraneless bodies spatially organize RNA splicing at their interfaces. This model explains how exon and intron binding by proteins positions splice sites for efficient splicing reactions.

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Membraneless bodies form through liquid-phase separation, crucial for nucleic acid biology.
Current models emphasize protein compartmentalization, overlooking other phase separation properties.
The functional roles of phase-separated body interfaces in organizing biochemical reactions are under-explored.

Purpose of the Study:

To propose a novel model for the nuclear speckle's function in RNA splicing.
To investigate the role of phase-separated body interfaces in spatially organizing biochemical reactions.
To explain the complex logic of RNA splicing through sequence-dependent RNA positioning.

Main Methods:

Developing a theoretical model for nuclear speckle function.
Analyzing the proposed binding interactions of SR proteins and hnRNP proteins with exons and introns, respectively.
Correlating RNA positioning at nuclear speckle interfaces with spliceosome accessibility.

Main Results:

Exons are sequestered into nuclear speckles via SR proteins, while introns are excluded by hnRNP proteins.
This differential binding positions splice sites at exon-intron boundaries at nuclear speckle interfaces.
Interface localization enhances splice site accessibility to spliceosomes, facilitating splicing.

Conclusions:

Phase-separated membraneless body interfaces can spatially organize biochemical reactions, exemplified by RNA splicing.
The proposed model explains key aspects of splicing, including factor duality and motif position dependence.
This interface-centric mechanism offers a new perspective on membraneless body function in nucleic acid biology.