TY - JOUR
T1 - Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea
AU - Suzuki, Tsutomu
AU - Ikeuchi, Yoshiho
AU - Kimura, Satoshi
AU - Numata, Tomoyuki
AU - Nakamura, Daigo
AU - Yokogawa, Takashi
AU - Ogata, Toshihiko
AU - Wada, Takeshi
AU - Suzuki, Takeo
N1 - Funding Information:
We are grateful to Y. Sakaguchi, T. Saigo, K. Nishikawa, S. Ohno and Y. Nomura for technical support and many fruitful discussions. Special thanks are due to Thermo Fischer Scientific for FT-MS analysis. This work was supported by Grants-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Science, Sports, and Culture of Japan (to Tsutomu Suzuki, T.Y. and T.W.); by a Japan Society for the Promotion of Science Fellowship for Japanese Junior Scientists (to Y.I.); by a PRESTO program grant from Japan Science and Technology (to T.N.) and by a grant from the New Energy and Industrial Technology Development Organization (NEDO) (to Tsutomu Suzuki).
PY - 2010/4
Y1 - 2010/4
N2 - A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAsIle with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm 2 C or agmatidine), at the wobble position of archaeal tRNA Ile that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm 2 C of tRNA Ile. We also identified a new enzyme, tRNA Ile -agm 2 C synthetase (TiaS), that catalyzes agm 2 C formation in the presence of agmatine and ATP. Although agm 2 C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNA Ile -lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
AB - A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAsIle with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm 2 C or agmatidine), at the wobble position of archaeal tRNA Ile that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm 2 C of tRNA Ile. We also identified a new enzyme, tRNA Ile -agm 2 C synthetase (TiaS), that catalyzes agm 2 C formation in the presence of agmatine and ATP. Although agm 2 C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNA Ile -lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
UR - http://www.scopus.com/inward/record.url?scp=77949820848&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77949820848&partnerID=8YFLogxK
U2 - 10.1038/nchembio.323
DO - 10.1038/nchembio.323
M3 - Article
C2 - 20139989
AN - SCOPUS:77949820848
SN - 1552-4450
VL - 6
SP - 277
EP - 282
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 4
ER -