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Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

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m⁶A Modified Short RNA Fragments Inhibit Cytoplasmic TLS/FUS Aggregation Induced by Hyperosmotic Stress.

Ryoma Yoneda¹, Naomi Ueda¹, Riki Kurokawa¹

¹Division of Biomedical Sciences, Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi, Saitama 350-1241, Japan.

International Journal of Molecular Sciences

|October 23, 2021

Summary

Translocated in Liposarcoma/Fused in Sarcoma (TLS/FUS) binds to m⁶A modified RNA, influencing its cellular localization and stress resistance. This suggests TLS/FUS is an m⁶A reader, with m⁶A RNA enhancing cell survival.

Keywords:

LLPS RNA m6A modification TLS/FUS lncRNA pncRNA-D

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Translocated in Liposarcoma/Fused in Sarcoma (TLS/FUS) is an RNA-binding protein implicated in amyotrophic lateral sclerosis.
TLS/FUS participates in liquid-liquid phase separation (LLPS) and forms membraneless organelles.
The impact of m⁶A RNA modification on TLS/FUS-RNA interactions is not well understood.

Purpose of the Study:

To investigate the binding specificity of TLS/FUS to m⁶A-modified RNAs.
To determine the functional consequences of m⁶A RNA interaction with TLS/FUS under stress conditions.

Main Methods:

RNA pull-down assays were used to assess TLS/FUS binding to m⁶A RNA fragments.
Cellular localization of TLS/FUS and stress resistance were evaluated after transfection with m⁶A-modified RNAs.

Main Results:

Both wild-type and ALS-mutant TLS/FUS proteins exhibit strong binding to m⁶A-modified RNAs.
m⁶A-modified RNA transfection reduced TLS/FUS cytoplasmic foci formation under hyperosmotic stress.
Cells transfected with m⁶A-modified RNAs showed increased resistance to hyperosmotic stress.

Conclusions:

TLS/FUS is identified as a novel m⁶A RNA recognition protein.
m⁶A-modified RNAs can diffuse TLS/FUS cytoplasmic foci, enhancing cellular viability under stress.