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

Matsushita, Yasuhiko; Ohshima, Mayumi; Yoshioka, K.; Nishiguchi, Masamichi; Nyunoya, Hiroshi

doi:10.1099/vir.0.18839-0

Cited by 39 publications

(20 citation statements)

References 34 publications

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“…A plant protein kinase with the biochemical properties of CK2 (formerly casein kinase II) has been shown to interact specifically with the MP of Tomato mosaic virus , a virus closely related to TMV, and to phosphorylate it in vitro ( Matsushita et al, 2000). This result was confirmed recently using the recombinant ␣ -catalytic subunit of CK2 from tobacco (Matsushita et al, 2003).…”

Section: Introductionsupporting

confidence: 66%

Phosphorylation of the Potyvirus Capsid Protein by Protein Kinase CK2 and Its Relevance for Virus Infection [W]

et al. 2003

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We reported previously that the capsid protein (CP) of Potato virus A (PVA) is phosphorylated both in virus-infected plants and in vitro. In this study, an enzyme that phosphorylates PVA CP was identified as the protein kinase CK2. The ␣ -catalytic subunit of CK2 (CK2 ␣ ) was purified from tobacco and characterized using in-gel kinase assays and liquid chromatographytandem mass spectrometry. The tobacco CK2 ␣ gene was cloned and expressed in bacterial cells. Specific antibodies were raised against the recombinant enzyme and used to demonstrate the colocalization of PVA CP and CK2 ␣ in infected tobacco protoplasts. A major site of CK2 phosphorylation in PVA CP was identified by a combination of mass spectrometric analysis, radioactive phosphopeptide sequencing, and mutagenesis as Thr-242 within a CK2 consensus sequence. Amino acid substitutions that affect the CK2 consensus sequence in CP were introduced into a full-length infectious cDNA clone of PVA tagged with green fluorescent protein. Analysis of the mutant viruses showed that they were defective in cell-to-cell and longdistance movement. Using in vitro assays, we demonstrated that CK2 phosphorylation inhibited the binding of PVA CP to RNA, suggesting a molecular mechanism of CK2 action. These results suggest that the phosphorylation of PVA CP by CK2 plays an important regulatory role in virus infection.

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Section: Introductionsupporting

confidence: 66%

Phosphorylation of the Potyvirus Capsid Protein by Protein Kinase CK2 and Its Relevance for Virus Infection [W]

et al. 2003

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“…Unlike studies of PVX viral movement and replication, interactions between PVX and host proteins are not well described. Among such studies the protein kinase CK2 was found to phosphorylate PVX TGB1 (Modena et al, 2008), as also reported for Tomato mosaic virus (ToMV) P30 movement protein (Lee 2008; Matsushita et al, 2003). In addition, another host protein, remorin (REM) which is located in the cytosolic leaflet of plasma membrane microdomains (lipid rafts) and in clusters at plasmodesmata (Pd), interacts with TGB1 to transport PVX to Pd (Raffaele et al, 2009).…”

supporting

confidence: 55%

Selective Interaction Between Chloroplast β-ATPase and TGB1L88 Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection

Seo

Nam

Kim

et al. 2014

The Plant Pathology Journal

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The multifunctional triple gene block protein 1 (TGB1) of the Potexvirus Alternanthera mosaic virus (AltMV) has been reported to have silencing suppressor, cell-to-cell movement, and helicase functions. Yeast two hybrid screening using an Arabidopsis thaliana cDNA library with TGB1 as bait, and co-purification with TGB1 inclusion bodies identified several host proteins which interact with AltMV TGB1. Host protein interactions with TGB1 were confirmed by biomolecular fluorescence complementation, which showed positive TGB1 interaction with mitochondrial ATP synthase delta′ chain subunit (ATP synthase delta′), light harvesting chlorophyll-protein complex I subunit A4 (LHCA4), chlorophyll a/b binding protein 1 (LHB1B2), chloroplast-localized IscA-like protein (ATCPISCA), and chloroplast β-ATPase. However, chloroplast β-ATPase interacts only with TGB1L88, and not with weak silencing suppressor TGB1P88. This selective interaction indicates that chloroplast β-ATPase is not required for AltMV movement and replication; however, TRV silencing of chloroplast β-ATPase in Nicotiana benthamiana induced severe tissue necrosis when plants were infected by AltMV TGB1L88 but not AltMV TGB1P88, suggesting that β-ATPase selectively responded to TGB1L88 to induce defense responses.

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“…Plant cell kinases mediate viral protein phosphorylation (1–16). The functional implications of the phosphorylation of nonstructural viral proteins have been elaborated (1–4,8–10,14,17–33), and the kinases involved have been characterized to some extent (4,5,7,8,12,13,15,21,27,28,34,35). Cell-to-cell movement of viruses involves the formation of a ribonucleoprotein (RNP) complex that interacts with host protein(s) to increase the size exclusion limit of plasmodesmata and to potentiate its own transport into neighboring cells (36,37).…”

Section: Introductionmentioning

confidence: 99%

“…Membrane association of TMV MP is eliminated by phosphorylation (24). In Tomato mosaic virus (ToMV) MP, Ser-28 and -37 are the preferable contexts for phosphorylation by casein kinase 2 (CK2), CK2-like protein kinase or recombinant N. tabacum RIO kinase (3,6,7,25). Ser-37 phosphorylation profoundly affects the cell-to-cell movement of the viral genome and the subcellular distribution of ToMV-MP (18).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complex

Vijayapalani

Chen

Liou

et al. 2011

Nucleic Acids Research

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Bamboo mosaic virus (BaMV) satellite RNA (satBaMV) depends on BaMV for its replication and encapsidation. SatBaMV-encoded P20 protein is an RNA-binding protein that facilitates satBaMV systemic movement in co-infected plants. Here, we examined phosphorylation of P20 and its regulatory functions. Recombinant P20 (rP20) was phosphorylated by host cellular kinase(s) in vitro, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and mutational analyses revealed Ser-11 as the phosphorylation site. The phosphor-mimic rP20 protein interactions with satBaMV-translated mutant P20 were affected. In overlay assay, the Asp mutation at S11 (S11D) completely abolished the self-interaction of rP20 and significantly inhibited the interaction with both the WT and S11A rP20. In chemical cross-linking assays, S11D failed to oligomerize. Electrophoretic mobility shift assay and subsequent Hill transformation analysis revealed a low affinity of the phospho-mimicking rP20 for satBaMV RNA. Substantial modulation of satBaMV RNA conformation upon interaction with nonphospho-mimic rP20 in circular dichroism analysis indicated formation of stable satBaMV ribonucleoprotein complexes. The dissimilar satBaMV translation regulation of the nonphospho- and phospho-mimic rP20 suggests that phosphorylation of P20 in the ribonucleoprotein complex converts the translation-incompetent satBaMV RNA to messenger RNA. The phospho-deficient or phospho-mimicking P20 mutant of satBaMV delayed the systemic spread of satBaMV in co-infected Nicotiana benthamiana with BaMV. Thus, satBaMV likely regulates the formation of satBaMV RNP complex during co-infection in planta.

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

Cited by 39 publications

References 34 publications

Phosphorylation of the Potyvirus Capsid Protein by Protein Kinase CK2 and Its Relevance for Virus Infection [W]

Phosphorylation of the Potyvirus Capsid Protein by Protein Kinase CK2 and Its Relevance for Virus Infection [W]

Selective Interaction Between Chloroplast β-ATPase and TGB1L88 Retards Severe Symptoms Caused by Alternanthera mosaic virus Infection

Phosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complex

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