Kengo Tsuda, Kanako Kuwasako, Mari Takahashi, Tatsuhiko Someya, Makoto Inoue, Takaho Terada, Naohiro Kobayashi, Mikako Shirouzu, Takanori Kigawa, Akiko Tanaka, Sumio Sugano, Peter Güntert, Yutaka Muto, Shigeyuki Yokoyama
- The CUG-binding protein 1 (CUG-BP1) is a member of the CUG-BP1 and ETR-like factors (CELF) family or the Bruno-like family and is involved in the control of splicing, translation and mRNA degradation. Several target RNA sequences of CUG-BP1 have been predicted, such as the CUG triplet repeat, the GU-rich sequences and the AU-rich element of nuclear pre-mRNAs and/or cytoplasmic mRNA. CUG-BP1 has three RNA-recognition motifs (RRMs), among which the third RRM (RRM3) can bind to the target RNAs on its own. In this study, we solved the solution structure of the CUG-BP1 RRM3 by hetero-nuclear NMR spectroscopy. The CUG-BP1 RRM3 exhibited a noncanonical RRM fold, with the four-stranded b-sheet surface tightly associated with the N-terminal extension. Furthermore, we determined the solution structure of the CUG-BP1 RRM3 in the complex with (UG)3 RNA, and discovered that the UGU trinucleotide is specifically recognized through extensive stacking interactions and hydrogen bonds within the pocket formed by the b-sheet surface and the N-terminal extension. This study revealed the unique mechanism that enables the CUG-BP1 RRM3 to discriminate the short RNA segment from other sequences, thus providing the molecular basis for the comprehension of the role of the RRM3s in the CELF/Bruno-like family.
MetadatenAuthor: | Kengo Tsuda, Kanako KuwasakoORCiD, Mari Takahashi, Tatsuhiko Someya, Makoto Inoue, Takaho Terada, Naohiro Kobayashi, Mikako Shirouzu, Takanori Kigawa, Akiko Tanaka, Sumio Sugano, Peter GüntertORCiDGND, Yutaka Muto, Shigeyuki Yokoyama |
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URN: | urn:nbn:de:hebis:30-68081 |
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DOI: | https://doi.org/10.1093/nar/gkp546 |
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ISSN: | 1362-4962 |
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ISSN: | 0305-1048 |
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Pubmed Id: | https://pubmed.ncbi.nlm.nih.gov/19553194 |
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Parent Title (English): | Nucleic acids research |
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Publisher: | Oxford Univ. Press |
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Place of publication: | Oxford |
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Document Type: | Article |
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Language: | English |
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Date of Publication (online): | 2009/08/10 |
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Date of first Publication: | 2009/06/24 |
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Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
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Release Date: | 2009/08/10 |
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Volume: | 37 |
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Issue: | 15 |
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Page Number: | 16 |
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First Page: | 5151 |
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Last Page: | 5166 |
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Note: | © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
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Source: | Nucleic Acids Research, 2009, 1–16 ; doi:10.1093/nar/gkp546 |
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HeBIS-PPN: | 214730492 |
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Institutes: | Biochemie, Chemie und Pharmazie / Biochemie und Chemie |
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| Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ) |
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Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Sammlungen: | Sammlung Biologie / Sondersammelgebiets-Volltexte |
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Licence (German): | Creative Commons - Namensnennung-Nicht kommerziell 2.0 |
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