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

 

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Opened Access A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein
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Author: Aroca Aguilar, Ángeles
Díaz Quintana, Antonio Jesús
Díaz Moreno, Irene
Department: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Date: 2011
Published in: FEBS Letters, 585 (19), 2958-2964.
Document type: Article
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 (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.
Cite: Aroca Aguilar, Á., Díaz Quintana, A.J. y Díaz Moreno, I. (2011). A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein. FEBS Letters, 585 (19), 2958-2964.
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URI: https://hdl.handle.net/11441/84563

DOI: 10.1016/j.febslet.2011.07.037

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