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
N1 - Funding Information:
We are grateful to the members of the Suzuki laboratory, particularly Y. Sakaguchi and T. Suzuki (University of Tokyo) for technical support and many fruitful discussions. We also thank H. Inanaga of the National Institute of Advanced Industrial Science and Technology (AIST) for technical assistance. 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 T.S.); by a Precursory Research for Embryonic Science and Technology (PRESTO) program grant from the Japan Science and Technology Agency (JST) (to T.N.); by a Japan Society for the Promotion of Science (JSPS) Fellowship for Japanese Junior Scientists (to T.O. and S.K.); by a Grant-in-Aid for Young Scientists from JSPS (to T.N.); and by a grant from the New Energy and Industrial Technology Development Organization (NEDO) (to T.S.).
PY - 2011/11
Y1 - 2011/11
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.
UR - http://www.scopus.com/inward/record.url?scp=80555131004&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80555131004&partnerID=8YFLogxK
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 Biology
JF - Nature Structural Biology
SN - 1545-9993
IS - 11
ER -