Phosphorylation of movement proteins by the plasmodesmal-associated protein kinase.
Plant viruses encode movement proteins (MPs) which play important roles in spreading their infectious materials throughout host plants. This infection is facilitated by cell-to-cell trafficking of MPs through specialized channels termed plasmodesmata, which involves specific interactions between MPs and host factors. Recently, we have reported the identification of a host protein kinase named plasmodesmal-associated protein kinase (PAPK) which specifically phosphorylates a subset of noncell autonomous proteins in vitro, including MPs of Tobacco mosaic virus (TMV) and Bean dwarf mosaic virus (BDMV). Biochemical purification of PAPK was achieved by developing a method in which a series of liquid chromatographic separations of plasmodesmal-enriched subcellular fractions was coupled with phosphorylation assays using TMV MP as a substrate. Application of this approach may prove useful in isolating other host kinases that interact with various viral components.
Lee
Jung-Youn
JY
Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, 15 Innovation Way, Newark, DE 19711, USA.
D018929:Cell Culture Techniques / Q000379:methods; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D009029:Mosaic Viruses / Q000201:enzymology; D010766:Phosphorylation; D053830:Plant Viral Movement Proteins / Q000302:isolation & purification / Q000378:metabolism*; D010942:Plant Viruses / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014027:Tobacco Mosaic Virus / Q000201:enzymology
D053830:Plant Viral Movement Proteins; D011494:Protein Kinases