Open AccessCauliflower mosaic virus coat protein is phosphorylated in vitro by a virion-associated protein kinase
Author(s) -
José Antonio Martı́nez-Izquierdo,
Thomas Höhn
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.7.1824
Subject(s) - protein kinase a , casein kinase 2 , biochemistry , biology , capsid , phosphorylation , casein kinase 2, alpha 1 , map2k7 , protein phosphorylation , c raf , casein kinase 1 , kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , microbiology and biotechnology , virology , virus
A protein kinase has been found to be associated with particles of the plant virus cauliflower mosaic virus. This protein kinase can phosphorylate endogenous viral capsid proteinsin vitro and exchange substrates with casein kinase type II. The activity is not affected by cAMP but is enhanced considerably by ADP. The cofactor is either Mn2+ or Mg2+ , and the phosphate donor is either ATP or GTP. Serine and threonine residues are phosphorylated.