TY  - JOUR
A1  - Tsuda, Kengo
A1  - Someya, Tatsuhiko
A1  - Kuwasako, Kanako
A1  - Takahashi, Mari
A1  - He, Fahu
A1  - Unzai, Satoru
A1  - Inoue, Makoto
A1  - Harada, Takushi
A1  - Watanabe, Satoru
A1  - Terada, Takaho
A1  - Kobayashi, Naohiro
A1  - Shirouzu, Mikako
A1  - Kigawa, Takanori
A1  - Tanaka, Akiko
A1  - Sugano, Sumio
A1  - Güntert, Peter
A1  - Yokoyama, Shigeyuki
A1  - Muto, Yutaka
T1  - Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM
T2  - Nucleic acids research
N2  - Human Transformer2-beta (hTra2-beta) is an important member of the serine/arginine-rich protein family, and contains one RNA recognition motif (RRM). It controls the alternative splicing of several pre-mRNAs, including those of the calcitonin/calcitonin gene-related peptide (CGRP), the survival motor neuron 1 (SMN1) protein and the tau protein. Accordingly, the RRM of hTra2-beta specifically binds to two types of RNA sequences [the CAA and (GAA)2 sequences]. We determined the solution structure of the hTra2-beta RRM (spanning residues Asn110–Thr201), which not only has a canonical RRM fold, but also an unusual alignment of the aromatic amino acids on the beta-sheet surface. We then solved the complex structure of the hTra2-beta RRM with the (GAA)2 sequence, and found that the AGAA tetra-nucleotide was specifically recognized through hydrogen-bond formation with several amino acids on the N- and C-terminal extensions, as well as stacking interactions mediated by the unusually aligned aromatic rings on the beta-sheet surface. Further NMR experiments revealed that the hTra2-beta RRM recognizes the CAA sequence when it is integrated in the stem-loop structure. This study indicates that the hTra2-beta RRM recognizes two types of RNA sequences in different RNA binding modes.
Y1  - 2010
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/20245
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30-85027
SN  - 1362-4962
SN  - 0305-1048
N1  - © The Author(s) 2010. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
VL  - 39
IS  - 4
SP  - 1538
EP  - 1553
PB  - Oxford Univ. Press
CY  - Oxford
ER  -