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A structural insight into the C‐terminal RNA recognition motifs of T‐cell intracellular antigen‐1 protein
Author(s) -
Aroca Ángeles,
Díaz-Quintana Antonio,
Díaz-Moreno Irene
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.07.037
Subject(s) - rna , rna recognition motif , rna splicing , intracellular , microbiology and biotechnology , messenger rna , translation (biology) , biology , biochemistry , biophysics , chemistry , gene
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.