テラチ トオル
TERACHI TORU
寺地 徹 所属 京都産業大学 生命科学部 産業生命科学科 職種 教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2004/10 |
形態種別 | その他 |
標題 | Cloning and characterization of a novel radish protein kinase which is homologous to fungal cot-I like and animal Ndr protein kinases |
執筆形態 | その他 |
掲載誌名 | GENES & GENETIC SYSTEMS |
出版社・発行元 | GENETICS SOC JAPAN |
巻・号・頁 | 79(5),pp.283-291 |
著者・共著者 | T Imai,S Shimamura,A Kurosaka,H Yamagishi,T Terachi |
概要 | According to the similarity of the amino acid sequences in their catalytic domains, eukaryotic protein kinases have been classified into the five main groups: 'AGC', 'CaMK', 'CMGC', 'PTK and 'other'. The AGC group, represented by the cyclic nucleotide-dependent kinases (PKA and PKG), the calcium-phospholipid-dependent kinases (PKC) and the ribosomal S6 protein kinases, are poorly characterized in plants except for a few cases. In this study, in order to gain a better understanding of plant protein kinases in the AGC group, three cDNAs encoding novel protein kinases, RsNdr1 and RsNdr2a/b, were cloned from radish and characterized by molecular and biochemical methods.
The deduced amino acid sequences of RsNdr1 and RsNdr2a/b contained all 12 conserved catalytic subdomains which are characteristic of the eukaryotic Ser/Thr protein kinases. A cell lysate from E. coli overexpressing RsNdr1 fusion protein had protein kinase activity toward a conventional protein substrate (myelin basic protein), whereas that from E. coli harboring a fusion plasmid encoding kinase-dead RsNdr1 or RsNdr2 did not show any protein kinase activity. A phylogenetic tree for 17 protein kinases from various organisms showed that the RsNdrs are more closely related to the protein kinases in a particular subgroup of the 'AGC' (fungal cot1-like and animal Ndr kinases) than to the authentic 'AGC' protein kinases, such as PKA, PKC or ribosomal S6 kinase. |
DOI | 10.1266/ggs.79.283 |
ISSN | 1341-7568/1880-5779 |