The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus

Yasuhiko Matsushita, Mayumi Ohshima, Kuniaki Yoshioka, Masamichi Nishiguchi, Hiroshi Nyunoya

Research output: Contribution to journalReview article

29 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)497-505
Number of pages9
JournalJournal of General Virology
Volume84
Issue number2
DOIs
Publication statusPublished - 2003 Feb 1
Externally publishedYes

ASJC Scopus subject areas

  • Virology

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