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FEBS Lett. 2011 Oct 3;585(19):2958-64. doi: 10.1016/j.febslet.2011.07.037. Epub 2011 Aug 11.

A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein.

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  • 1Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Sevilla, Spain.

Abstract

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 α-helix (α(1)) which protects its single tryptophan from the solvent exposure, even in the two-domain RRM23 context. The α(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.

Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

PMID:
21846467
[PubMed - indexed for MEDLINE]
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