The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus
| Autor: | Mayumi Ohshima, Kuniaki Yoshioka, Hiroshi Nyunoya, Yasuhiko Matsushita, Masamichi Nishiguchi |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
animal structures
Recombinant Fusion Proteins Molecular Sequence Data macromolecular substances Protein Serine-Threonine Kinases Biology Mitogen-activated protein kinase kinase MAP2K7 Viral Proteins Catalytic Domain Virology Casein kinase 2 alpha 1 Cloning Molecular Phosphorylation Casein Kinase II Protein kinase A Glutathione Transferase MAP kinase kinase kinase Tobamovirus fungi Cyclin-dependent kinase 2 Sequence Analysis DNA Molecular biology Plant Viral Movement Proteins Biochemistry embryonic structures biology.protein Cyclin-dependent kinase 9 Casein kinase 2 |
| Zdroj: | Journal of General Virology. 84:497-505 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.18839-0 |
| Popis: | The movement protein (MP) of Tomato mosaic virus (ToMV) was reported previously by us to be phosphorylated in vitro by a cellular protein kinase(s) that exhibited several characteristics of casein kinase 2 (CK2). To characterize further this CK2-like cellular kinase, we have cloned cDNAs encoding the CK2 catalytic subunit from tobacco and compared the properties of the recombinant protein with those of the CK2-like cellular kinase. The recombinant CK2 catalytic subunit formed a complex with ToMV MP and phosphorylated it, similar to the CK2-like cellular kinase. Phosphoamino acid analyses of various mutant MPs altered near the C terminus revealed that the recombinant CK2 catalytic subunit phosphorylated serine-261, while the CK2-like cellular kinase phosphorylated both serine-261 and threonine-256. Both kinases were suggested to phosphorylate an additional serine residue(s) in regions other than the C-terminal peptide. The results are consistent with our previous prediction of involvement of CK2 in phosphorylation of ToMV MP. |
| Databáze: | OpenAIRE |
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