What question did this study set out to answer?

This research aims to understand how Arg-rich proteins unfold RNA G-quadruplexes and their implications for RNA processing.

June 15, 2026Open Access

Sequence Determinants of RNA G-Quadruplex Unfolding by Arg-Rich Regions

Key Points

This research aims to understand how Arg-rich proteins unfold RNA G-quadruplexes and their implications for RNA processing.
Investigated the unfolding activity of SR and Arg-rich proteins on RNA G-quadruplex structures.
Identified requirements, such as the number of Arg residues needed to unfold specific rGQs.
Identified that at least 13 Arg residues are needed to unfold the ARPC2 rGQ.
Demonstrated that Arg residues are key drivers of unfolding while acidic residues reduce activity.
Revealed Arg-rich proteins act as helicase-independent regulators of rGQ structures.

Abstract

RNA sequences with the potential to form G-quadruplexes (rGQs) are widespread but largely unfolded in cells by unknown mechanisms. rGQ folding status is a critical regulator of RNA splicing and translation. We show that rGQs can be unfolded by SR proteins, SR-related proteins, and other Arg-rich proteins, including SRSF1, SRSF3, SRSF9, U1-70K, and U2AF1. The length and composition of Arg-rich regions are key determinants of this activity: Arg residues are the primary drivers, while acidic residues attenuate the unfolding activity. To unfold ARPC2 rGQ, at least 13 Arg residues are required. Our findings identify Arg-rich proteins as previously unrecognized, helicase-independent regulators of rGQ structures, with potential broad impacts on RNA processing that merit further investigation.

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