Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS

Naohiro Terasaka, Satoshi Kimura, Takuo Osawa, Tomoyuki Numata, Tsutomu Suzuki

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The archaeal AUA-codon specific tRNA Ile contains 2-agmatinylcytidine (agm 2 C or agmatidine) at the anticodon wobble position (position 34). The formation of this essential modification is catalyzed by tRNA Ile-agm 2 C synthetase (TiaS) using agmatine and ATP as substrates. TiaS has a previously unknown catalytic domain, which we have named the Thr18-Cyt34 kinase domain (TCKD). Biochemical analyses of Archaeoglobus fulgidus TiaS and its mutants revealed that the TCKD first hydrolyzes ATP into AMP and pyrophosphate, then phosphorylates the C2 position of C34 with the Î 3-phosphate. Next, the amino group of agmatine attacks this position to release the phosphate and form agm 2 C. Notably, the TCKD also autophosphorylates the Thr18 of TiaS, which may be involved in agm 2 C formation. Thus, the unique kinase domain of TiaS catalyzes dual phosphorylation of protein and RNA substrates.

Original languageEnglish
Pages (from-to)1268-1274
Number of pages7
JournalNature Structural and Molecular Biology
Volume18
Issue number11
DOIs
Publication statusPublished - Nov 1 2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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