English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/75786
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

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
PublisherElsevier
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
URIhttp://hdl.handle.net/10261/75786
DOIhttp://dx.doi.org/10.1016/j.febslet.2011.07.037
ISSN0014-5793
Appears in Collections:(IBVF) Artículos
Files in This Item:
File Description SizeFormat 
FEBS Letters Volume 585, Issue 19, 3 October 2011, Pages 2958–2964.docx346,88 kBMicrosoft Word XMLView/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.