Journal
FEBS LETTERS
Volume 585, Issue 19, Pages 2958-2964Publisher
WILEY
DOI: 10.1016/j.febslet.2011.07.037
Keywords
DNA-RNA binding protein (D/RBP); RNA metabolism; RNA recognition motif (RRM); Pro-apoptotic protein; T-cell-restricted intracellular antigen-1 (TIA-1)
Funding
- Andalusian Government [P07-CVI-02896, BIO198]
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T-cell intracellular antigen-1 (TIA-1) plays a pleiotropic role in cell homeostasis through the regulation of alternative pre-mRNA splicing and mRNA translation by recognising uridine-rich sequences of RNAs. TIA-1 contains three RNA recognition motifs (RRMs) and a glutamine-rich domain. Here, we characterise its C-terminal RRM2 and RRM3 domains. Notably, RRM3 contains an extra novel N-terminal alpha-helix (alpha(1)) which protects its single tryptophan from the solvent exposure, even in the two-domain RRM23 context. The alpha(1) hardly affects the thermal stability of RRM3. On the contrary, RRM2 destabilises RRM3, indicating that both modules are tumbling together, which may influence the RNA binding activity of TIA-1. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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