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

被引：18

作者：

Terasaka, Naohiro ^{[1
]}

Kimura, Satoshi ^{[1
]}

Osawa, Takuo ^{[2
]}

Numata, Tomoyuki ^{[2
,3
]}

Suzuki, Tsutomu ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Engn, Dept Chem & Biotechnol, Tokyo, Japan

[2] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, Ibaraki, Japan

[3] Japan Sci & Technol Agcy JST, Precursory Res Embryon Sci & Technol PRESTO, Saitama, Japan

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 11期

基金：

日本学术振兴会; 日本科学技术振兴机构;

关键词：

AMINO-ACID SPECIFICITIES; SULFUR-RELAY; CODON; ANTICODON; AGMATINE; CYTIDINE; ENZYME;

D O I：

10.1038/nsmb.2121

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 gamma-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.

引用

页码：1268 / U116

页数：8

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