Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNATyr with an extra guanosine residue at the 5'-terminus.

Tatsuya Horikoshi, Hiroki Noguchi, Takuya Umehara, Hiromi Mutsuro-Aoki, Ryodai Kurihara, Ryohei Noguchi, Takahiro Hashimoto, Yuki Watanabe, Tadashi Ando, Kenichi Kamata, Sam-Yong Park, Koji Tamura

Biochemical and biophysical research communications 2021 Oct 20

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tRNATyr of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNATyr mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å 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 5'-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. Copyright © 2021 Elsevier Inc. All rights reserved.

Citation

Tatsuya Horikoshi, Hiroki Noguchi, Takuya Umehara, Hiromi Mutsuro-Aoki, Ryodai Kurihara, Ryohei Noguchi, Takahiro Hashimoto, Yuki Watanabe, Tadashi Ando, Kenichi Kamata, Sam-Yong Park, Koji Tamura. Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNATyr with an extra guanosine residue at the 5'-terminus. Biochemical and biophysical research communications. 2021 Oct 20;575:90-95