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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hirano, Nagisa Yu, Futao Tanaka, Isao Suzuki, Takeo Yamashita, Keitaro Suzuki, Tsutomu Tanaka, Yoshikazu Yao, Min Nakamura, Akiyoshi |
| Description | Author Affiliation: Yu F ( Graduate School of Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.); |
| Abstract | Dihydrouridine (D) is a highly conserved modified base found in tRNAs from all domains of life. Dihydrouridine synthase (Dus) catalyzes the D formation of tRNA through reduction of uracil base with flavin mononucleotide (FMN) as a cofactor. Here, we report the crystal structures of Thermus thermophilus Dus (TthDus), which is responsible for D formation at positions 20 and 20a, in complex with tRNA and with a short fragment of tRNA (D-loop). Dus interacts extensively with the D-arm and recognizes the elbow region composed of the kissing loop interaction between T- and D-loops in tRNA, pulling U20 into the catalytic center for reduction. Although distortion of the D-loop structure was observed upon binding of Dus to tRNA, the canonical D-loop/T-loop interaction was maintained. These results were consistent with the observation that Dus preferentially recognizes modified rather than unmodified tRNAs, indicating that Dus introduces D20 by monitoring the complete L-shaped structure of tRNAs. In the active site, U20 is stacked on the isoalloxazine ring of FMN, and C5 of the U20 uracil ring is covalently cross linked to the thiol group of Cys93, implying a catalytic mechanism of D20 formation. In addition, the involvement of a cofactor molecule in uracil ring recognition was proposed. Based on a series of mutation analyses, we propose a molecular basis of tRNA recognition and D formation catalyzed by Dus. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 49 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Oxidoreductases RNA, Transfer Uridine Amino Acid Sequence Genetics Metabolism Binding Sites Biocatalysis Crystallography, X-Ray Electrophoresis, Polyacrylamide Gel Flavin Mononucleotide Models, Molecular Molecular Sequence Data Mutation Nucleic Acid Conformation Oxidation-Reduction Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Thermus Thermophilus Enzymology Uracil Analogs & Derivatives Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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