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

AuthorsAroca, Ángeles CSIC ORCID; Díaz-Quintana, Antonio; Díaz-Moreno, Irene CSIC ORCID
KeywordsDNA–RNA binding protein (D/RBP)
RNA metabolism
RNA recognition motif (RRM)
Pro-apoptotic protein
T-cell-restricted intracellular antigen-1 (TIA-1)
Issue Date3-Oct-2011
CitationFEBS Letters 585 (19): 2958–2964 (2011).
AbstractT-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 (α1) which protects its single tryptophan from the solvent exposure, even in the two-domain RRM23 context. The α1 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.
Description7 Páginas, 5 figuras
Publisher version (URL)http://dx.doi.org/10.1016/j.febslet.2011.07.037
Appears in Collections:(IBVF) Artículos
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