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PMID: 20139989 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea.

Nature chemical biology ·Vol. 6 ·No. 4 ·2010-04-00 ·Pages 277-82

Ikeuchi Y, Kimura S, Numata T, Nakamura D, Yokogawa T, Ogata T, Wada T, Suzuki T, Suzuki T

Abstract

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.

MeSH Terms
Agmatine/chemistry,metabolism Anticodon/chemistry,genetics,metabolism Archaea/cytology,genetics,metabolism Catalysis Cytidine/chemistry,metabolism Ligases/metabolism RNA, Transfer/chemistry,genetics,metabolism
Chemicals
Anticodon Cytidine Agmatine RNA, Transfer Ligases
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Ikeuchi Yoshiho
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
Kimura Satoshi
Numata Tomoyuki
Nakamura Daigo
Yokogawa Takashi
Ogata Toshihiko
Wada Takeshi
Suzuki Takeo
Suzuki Tsutomu
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Article Info
Journal
Nature chemical biology
Abbr.
Nat Chem Biol
ISSN
1552-4469
DOI
10.1038/nchembio.323
Published
2010-04-00
Epub
2010-00-07
Pages
277-82
Language
English
Region
United States
NLM ID
101231976
Subset
IM
Databases
PubChem-Substance
87326004, 87326005, 87326006, 87326007, 87326008
External Links
PubMed source DOI: 10.1038/nchembio.323 View journal details
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