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RNA Binding of T-cell Intracellular Antigen-1 (TIA-1) C-terminal RNA Recognition Motif Is Modified by pH Conditions

Journal article
Authors I. Cruz-Gallardo
A. Aroca
Cecilia Persson
B Göran Karlsson
I. Diaz-Moreno
Published in Journal of Biological Chemistry
Volume 288
Issue 36
Pages 25986-25994
ISSN 0021-9258
Publication year 2013
Published at Swedish NMR Centre at Göteborg University
Pages 25986-25994
Language en
Links dx.doi.org/10.1074/jbc.M113.489070
Keywords MAMMALIAN STRESS GRANULES, MESSENGER-RNAS, PROTEIN COMPLEX, DOMAIN, NMR, PHOSPHORYLATION, IDENTIFICATION, HEMAGGLUTININ, RECRUITMENT, REGULATOR
Subject categories Biochemistry

Abstract

T-cell intracellular antigen-1 (TIA-1) is a DNA/RNA-binding protein that regulates critical events in cell physiology by the regulation of pre-mRNA splicing and mRNA translation. TIA-1 is composed of three RNA recognition motifs (RRMs) and a glutamine-rich domain and binds to uridine-rich RNA sequences through its C-terminal RRM2 and RRM3 domains. Here, we show that RNA binding mediated by either isolated RRM3 or the RRM23 construct is controlled by slight environmental pH changes due to the protonation/deprotonation of TIA-1 RRM3 histidine residues. The auxiliary role of the C-terminal RRM3 domain in TIA-1 RNA recognition is poorly understood, and this work provides insight into its binding mechanisms.

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