%0 Journal Article %A Matsushita, Yasuhiko %A Ohshima, Mayumi %A Yoshioka, Kuniaki %A Nishiguchi, Masamichi %A Nyunoya, Hiroshi %T The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus %D 2003 %J Journal of General Virology, %V 84 %N 2 %P 497-505 %@ 1465-2099 %R https://doi.org/10.1099/vir.0.18839-0 %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.18839-0