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Phosphorylation Regulates the Subcellular Localization of Cucumber Mosaic Virus 2b Protein

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Journal Sci Rep
Specialty Science
Date 2017 Oct 19
PMID 29044170
Citations 14
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Abstract

The 2b protein of Cucumber mosaic virus has a role in nearly all steps of the viral cycle including cell-to-cell movement, symptom induction and suppression of antiviral RNA silencing. Previous studies demonstrated the presence of 2b protein in the nucleus and in cytoplasm as well. Phosphorylation site of 2b protein is conserved in all CMV isolates, including proposed constitute motifs for casein kinase II and cyclin-dependent kinase 2. To discern the impact of 2b protein phosphorylation, we created eight different mutants to mimic the non-phosporylated (serine to alanine) as well as the phosphorylated state (serine to aspartic acid) of the protein. We compared these mutants to the wild-type (Rs-CMV) virus in terms of symptom induction, gene silencing suppressor activity as well as in cellular localization. Here, in this study we confirmed the phosphorylation of 2b protein in vivo, both in infected N. benthamiana and in infiltrated patches. Mutants containing aspartic acid in the phosphorylation site accumulated only in the cytoplasm indicating that phosphorylated 2b protein could not enter the nucleus. We identified a conserved dual phosphorylation switch in CMV 2b protein, which equilibrates the shuttling of the 2b protein between the nucleus and the cytoplasm, and regulates the suppressor activity of the 2b protein.

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References
1.
Khoury G, Baliban R, Floudas C . Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci Rep. 2011; 1. PMC: 3201773. DOI: 10.1038/srep00090. View

2.
Karger E, Frolova O, Fedorova N, Baratova L, Ovchinnikova T, Susi P . Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation. J Gen Virol. 2003; 84(Pt 3):727-732. DOI: 10.1099/vir.0.18972-0. View

3.
Zhang S, Klessig D . Resistance gene N-mediated de novo synthesis and activation of a tobacco mitogen-activated protein kinase by tobacco mosaic virus infection. Proc Natl Acad Sci U S A. 1998; 95(13):7433-8. PMC: 22641. DOI: 10.1073/pnas.95.13.7433. View

4.
Cohen P . The regulation of protein function by multisite phosphorylation--a 25 year update. Trends Biochem Sci. 2000; 25(12):596-601. DOI: 10.1016/s0968-0004(00)01712-6. View

5.
Sessa G, DAscenzo M, Martin G . Thr38 and Ser198 are Pto autophosphorylation sites required for the AvrPto-Pto-mediated hypersensitive response. EMBO J. 2000; 19(10):2257-69. PMC: 384356. DOI: 10.1093/emboj/19.10.2257. View