Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM

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

Ethics of Information Education for Living with Robots

ICT drastically changes our lifestyle. Education must keep up with the change to have our next generation to survive. This paper will first point out lack of unanimous ethical guideline on ICT with illustrations from the current educational practices in Japan, then claim that coherent policies need a coherent conceptual system. As any guidelines of information education reflect a value system, or ethical bases of our decision making, it is essential to invite civilians and non-professionals of ICT to commit themselves in research, development, and education from the early stages

3P067 Natural Design in Controlling Dimerization of a Protein Module : Lessons from the WW domains(Proteins-stability, folding, and other physicochemical properties,Oral Presentations)

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