2RNE

Solution structure of the second RNA recognition motif (RRM) of TIA-1

Summary for 2RNE

• Entry DOI: 10.2210/pdb2rne/pdb
• NMR Information: BMRB: 11370,11371,11372,11373,11374,11375,11376
• Descriptor: Tia1 protein (1 entity in total)
• Functional Keywords: rrm domain, rna binding protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 12432.72

Authors

Takahashi, M.,Kuwasako, K.,Abe, C.,Tsuda, K.,Inoue, M.,Terada, T.,Shirouzu, M.,Kobayashi, N.,Kigawa, T.,Taguchi, S.,Guntert, P.,Hayashizaki, Y.,Tanaka, A.,Muto, Y.,Yokoyama, S. (deposition date: 2007-12-19, release date: 2008-11-04, Last modification date: 2024-05-29)

Primary citation

Kuwasako, K.,Takahashi, M.,Tochio, N.,Abe, C.,Tsuda, K.,Inoue, M.,Terada, T.,Shirouzu, M.,Kobayashi, N.,Kigawa, T.,Taguchi, S.,Tanaka, A.,Hayashizaki, Y.,Guntert, P.,Muto, Y.,Yokoyama, S.
Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode
Biochemistry, 47:6437-6450, 2008

PubMed Abstract: T cell intracellular antigen-1 (TIA-1), an apoptosis promoting factor, functions as a splicing regulator for the Fas pre-mRNA. TIA-1 possesses three RNA recognition motifs (RRMs) and a glutamine-rich domain. The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5' splice sites. In the present study, we solved the solution structure of the murine TIA-1 RRM2 by heteronuclear-nuclear magnetic resonance spectroscopy. The TIA-1 RRM2 adopts the RRM fold (betaalphabetabetaalphabeta) and possesses an extra beta-strand between beta2 and beta3, which forms an additional beta-sheet with the C-terminal part of beta2. We refer to this structure as the beta2-beta2' beta-loop. Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs. Furthermore, we identified a new sequence motif in the beta2-beta2' beta-loop, the DxxT motif. Chemical shift perturbation analyses of both the main and side chains upon binding to the uridine pentamer RNA revealed that most of the beta-sheet surface, including the beta2-beta2' beta-loop, is involved in the RNA binding. An investigation of the chemical shift perturbation revealed similarity in the RNA recognition modes between the TIA-1 and U2AF65 RRMs.

PubMed: 18500819
DOI: 10.1021/bi7024723

Experimental method

SOLUTION NMR