1. Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNATyr with an extra guanosine residue at the 5ʹ-terminus
- Author
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Ryohei Noguchi, Tadashi Ando, Takahiro Hashimoto, Tatsuya Horikoshi, Sam-Yong Park, Ryodai Kurihara, Takuya Umehara, Kenichi Kamata, Hiromi Mutsuro-Aoki, Yuki Watanabe, Koji Tamura, and Hiroki Noguchi
- Subjects
biology ,Base pair ,Stereochemistry ,Mutant ,Biophysics ,Guanosine ,Methanocaldococcus jannaschii ,Aminoacylation ,Cell Biology ,Thermus thermophilus ,biology.organism_classification ,environment and public health ,Biochemistry ,enzymes and coenzymes (carbohydrates) ,chemistry.chemical_compound ,chemistry ,parasitic diseases ,Transfer RNA ,Nanoarchaeum equitans ,Molecular Biology - Abstract
tRNATyr of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5ʹ-terminus. However, the N. equitans tRNATyr mutant without extra guanosine at the 5ʹ-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 A resolution. By comparing the present solved structure with the complex structures TyrRS with tRNATyr of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5ʹ-phosphate of C1 of N. equitans tRNATyr, was prepared. The I200R mutant tyrosylated not only wild-type tRNATyr but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites.
- Published
- 2021