ArticleBiochemical and biophysical research communications2008
Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- The Multifunctional Faces of T-Cell Intracellular Antigen 1 in Health and Disease.International journal of molecular sciences · 2022Review
- The Stress Granule RNA-Binding Protein TIAR-1 Protects Female Germ Cells from Heat Shock in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2016Article
- T-cell intracellular antigens in health and disease.Cell cycle (Georgetown, Tex.) · 2015Review
- Article
- RNA recognition and stress granule formation by TIA proteins.International journal of molecular sciences · 2014Review
- Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1.Nucleic acids research · 2014Article
- The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain.RNA biology · 2014Article
- RNA binding of T-cell intracellular antigen-1 (TIA-1) C-terminal RNA recognition motif is modified by pH conditions.The Journal of biological chemistry · 2013Article
- Distinct binding properties of TIAR RRMs and linker region.RNA biology · 2013Article
- Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.Journal of molecular biology · 2012Article
- Determinants of Nam8-dependent splicing of meiotic pre-mRNAs.Nucleic acids research · 2011Article
- An RNA recognition motif mediates the nucleocytoplasmic transport of a trypanosome RNA-binding protein.The Journal of biological chemistry · 2009Article
- The pivotal roles of TIA proteins in 5' splice-site selection of alu exons and across evolution.PLoS genetics · 2009Article
- Crystallization and preliminary crystallographic analysis of the second RRM of Pub1 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
T-cell-restricted intracellular antigen-1 (TIA-1) regulates alternative pre-mRNA splicing in the nucleus, and mRNA translation in the cytoplasm, by recognizing uridine-rich sequences of RNAs. As a step towards understanding RNA recognition by this regulatory factor, the X-ray structure of the central RNA recognition motif (RRM2) of human TIA-1 is presented at 1.95A resolution. Comparison with structurally homologous RRM-RNA complexes identifies residues at the RNA interfaces that are conserved in TIA-1-RRM2. The versatile capability of RNP motifs to interact with either proteins or RNA is reinforced by symmetry-related protein-protein interactions mediated by the RNP motifs of TIA-1-RRM2. Importantly, the TIA-1-RRM2 structure reveals the locations of mutations responsible for inhibiting nuclear import. In contrast with previous assumptions, the mutated residues are buried within the hydrophobic interior of the domain, where they would be likely to destabilize the RRM fold rather than directly inhibit RNA binding.
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