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 language | English |
|---|---|
| Pages (from-to) | 1268-1274 |
| Number of pages | 7 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 18 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 1 2011 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
Cite this
Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS. / Terasaka, Naohiro; Kimura, Satoshi; Osawa, Takuo; Numata, Tomoyuki; Suzuki, Tsutomu.
In: Nature Structural and Molecular Biology, Vol. 18, No. 11, 01.11.2011, p. 1268-1274.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS
AU - Terasaka, Naohiro
AU - Kimura, Satoshi
AU - Osawa, Takuo
AU - Numata, Tomoyuki
AU - Suzuki, Tsutomu
PY - 2011/11/1
Y1 - 2011/11/1
N2 - 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.
AB - 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.
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U2 - 10.1038/nsmb.2121
DO - 10.1038/nsmb.2121
M3 - Article
C2 - 22002222
AN - SCOPUS:80555131004
VL - 18
SP - 1268
EP - 1274
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 11
ER -