Phosphorylation of tobacco mosaic virus cell-to-cell movement protein by a developmentally regulated plant cell wall-associated protein kinase.

Citovsky, Vitaly; McLean, Barbara; Zupan, John R.; Zambryski, P

doi:10.1101/gad.7.5.904

Cited by 169 publications

(124 citation statements)

References 39 publications

(43 reference statements)

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“…Coat proteins (CPs) of the Cauliflower mosaic virus (Martinez-Izquierdo and Hohn, 1987) and potyviruses (Ivanov et al, 2001;Fernández-Fernández et al, 2002) as well as movement protein (MP) of Tobacco mosaic virus (Atkins et al, 1991;Watanabe et al, 1992;Citovsky et al, 1993;Waigmann et al, 2000) are phosphorylated, and several functions of these proteins are affected by phosphorylation (Karpova et al, 1999;Kawakami et al, 1999;Waigmann et al, 2000). Previous studies also identified a PERK-Like Receptor Kinase, NsAK, that may regulate nuclear shuttle protein function through phosphorylation (Florentino et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Tomato SlSnRK1 Protein Interacts with and Phosphorylates βC1, a Pathogenesis Protein Encoded by a Geminivirus β-Satellite

et al. 2011

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The bC1 protein of tomato yellow leaf curl China b-satellite functions as a pathogenicity determinant. To better understand the molecular basis of bC1 in pathogenicity, a yeast two-hybrid screen of a tomato (Solanum lycopersicum) cDNA library was carried out using bC1 as bait. bC1 interacted with a tomato SUCROSE-NONFERMENTING1-related kinase designated as SlSnRK1. Their interaction was confirmed using a bimolecular fluorescence complementation assay in Nicotiana benthamiana cells. Plants overexpressing SnRK1 were delayed for symptom appearance and contained lower levels of viral and satellite DNA, while plants silenced for SnRK1 expression developed symptoms earlier and accumulated higher levels of viral DNA. In vitro kinase assays showed that bC1 is phosphorylated by SlSnRK1 mainly on serine at position 33 and threonine at position 78. Plants infected with bC1 mutants containing phosphorylation-mimic aspartate residues in place of serine-33 and/or threonine-78 displayed delayed and attenuated symptoms and accumulated lower levels of viral DNA, while plants infected with phosphorylation-negative alanine mutants contained higher levels of viral DNA. These results suggested that the SlSnRK1 protein attenuates geminivirus infection by interacting with and phosphorylating the bC1 protein.

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Section: Discussionmentioning

confidence: 99%

Tomato SlSnRK1 Protein Interacts with and Phosphorylates βC1, a Pathogenesis Protein Encoded by a Geminivirus β-Satellite

et al. 2011

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“…If this is also true for the ORF2 products of potexviruses, the apparent abundance of these proteins in inclusions in infected tissue would be more reasonable. However, it may also be possible that the EDCBs we observed, as well as those for PVX and FMV, are repositories for excess amounts of ORF2 products in infected plants, as suggested by Citovsky et al (1993). Therefore, the location of 28 kDa protein does not necessarily reflect the area in which it has a function.…”

mentioning

confidence: 79%

Subcellular localization of the 28 kDa protein of the triple-gene-block of bamboo mosaic potexvirus.

Chang

Lin

Liou

et al. 1997

Journal of General Virology

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Open reading frame 2 of the bamboo mosaic potexvirus (BaMV) genome encodes a 28 kDa protein, the first of the ' triple-gene-block ' of BaMV which is believed to play a role in cell-to-cell movement of the virus in host plants. The 28 kDa protein was expressed in Escherichia coli and polyclonal antiserum was raised in a rabbit. Western blot analyses showed that the 28 kDa protein was associated mainly with components in the cell wall and 30 000 g pellet fractions of a BaMV-infected leaf homogenate. Immunogold electron microscopy of infected leaf tissues revealed that the 28 kDa protein was associated with electron-dense crystalline bodies (EDCBs) in the cytoplasm and nuclei. Nuclear EDCBs were found closely associated with nucleoli. Gold-labelled EDCB-like structures were also detected in the cytoplasm, but not within nuclei, in protoplasts up to 48 h post-inoculation. No specific labelling of the 28 kDa protein was found within any cytoplasmic structures or within cell walls.

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“…Young leaves of N. benthamiana or N. tabacum were infected mechanically with TMV (10 mg ml 21 ) or agroinjected with MP expression vector (Tyulkina et al, 2006). At different times post-inoculation (from 1 to 5 days), the leaves were treated as described by Citovsky et al (1993) with slight modifications. All operations were carried out at 4 uC.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Non-phosphorylatable mutants (del 43, sb3A) were movement-competent in N. tabacum and N. benthamiana Trutnyeva et al, 2005). Therefore, C-terminal phosphorylation was suggested to represent a host-dependent regulatory mechanism for inactivating the MP gating function in order to minimize detrimental effects of MP on host metabolism (Citovsky et al, 1993;Waigmann et al, 2000).It cannot be ruled out that phosphorylation of MP may control certain steps of the virus life cycle, acting as a molecular device to regulate virus spread and replication/ translation events (Lee & Lucas, 2001;Rhee et al, 2000). It has been reported that 'informosome'-like ribonucleoprotein (RNP) complexes, presumably formed in vivo, could be isolated from TMV-infected plants (Dorokhov et al, 1983(Dorokhov et al, , 1984.…”

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confidence: 99%

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Binding of monoclonal antibodies to the movement protein (MP) of Tobacco mosaic virus: influence of subcellular MP localization and phosphorylation

Tyulkina

Karger

Sheveleva

et al. 2010

Journal of General Virology

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Monoclonal antibodies (mAbs) to recombinant movement protein (MP REC ) of Tobacco mosaic virus (TMV) were used to reveal the dependence of MP epitope accessibility to mAbs on subcellular MP localization and post-translational MP phosphorylation. Leaves of Nicotiana benthamiana or N. tabacum were inoculated mechanically with TMV or agroinjected with an MP expression vector. At different time post-inoculation, ER membrane-and cell wall-enriched fractions (ER-MP and CW-MP, respectively) were isolated and analysed. The N-terminal region (residues 1-30) as well as regions 186-222 and 223-257 of MP from the CW and ER fractions were accessible for interaction with mAbs. By contrast, the MP regions including residues 76-89 and 98-129 were not accessible. The C-terminal TMV MP region (residues 258-268) was inaccessible to mAbs not only in CW-MP, but also in ER-MP fractions. Evidence is presented that phosphorylation of the majority of TMV MP C-terminal sites occurred on ER membranes at an early stage of virus infection, i.e. not after, but before reaching the cell wall. C-terminal phosphorylation of purified MP REC abolished recognition of C-proximal residues 258-268 by specific mAbs, which could be restored by MP dephosphorylation. Likewise, accessibility to mAbs of the C-terminal MP epitope in ER-MP and CW-MP leaf fractions was restored by dephosphorylation. Substitution of three or four C-terminal Ser/Thr residues with nonphosphorylatable Ala also resulted in abolition of interaction of mAbs with MP. INTRODUCTIONThe movement protein (MP) of Tobacco mosaic virus (TMV) facilitates movement of the virus genome within and between cells (for reviews, see Citovsky, 1999;Heinlein & Epel, 2004;Lucas, 2006). Polyfunctional TMV MP plays a key role in virus infection. It increases the size exclusion limit of plasmodesmata (PD) (Tomenius et al., 1987;Deom et al., 1987;Wolf et al., 1989), serves as an anchor of the viral genomic RNA to the ER (Mas & Beachy, 1999) and plays an important role in intracellular transport of replication complexes Kawakami et al., 2004). Unlike other TMV proteins, the MP is produced transiently in the early stages of virus infection (Watanabe et al., 1984;Lehto et al., 1990). Within the infected cell, MP is synthesized at the leading edge and degraded at the trailing edge of the infection site (Padgett et al., 1996). Polyubiquitination of MP and subsequent degradation by the 26S proteasome pathway occurs after the early stages of infection (Reichel & Beachy, 2000). However, the mechanisms responsible for the regulation of transient MP expression are not clear.Post-translational modifications, in particular phosphorylation/dephosphorylation, are important in regulation of gene expression and protein activity. It is known that, during virus infection, TMV MP undergoes phosphorylation by a cellular protein kinase(s). It has been shown that multiple phosphorylation events in internal regions of TMV MP occur in TMV-infected protoplasts (Haley et al., 1995). On the other hand, only three C-terminal residues o...

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Phosphorylation of tobacco mosaic virus cell-to-cell movement protein by a developmentally regulated plant cell wall-associated protein kinase.

Cited by 169 publications

References 39 publications

Tomato SlSnRK1 Protein Interacts with and Phosphorylates βC1, a Pathogenesis Protein Encoded by a Geminivirus β-Satellite

Tomato SlSnRK1 Protein Interacts with and Phosphorylates βC1, a Pathogenesis Protein Encoded by a Geminivirus β-Satellite

Subcellular localization of the 28 kDa protein of the triple-gene-block of bamboo mosaic potexvirus.

Binding of monoclonal antibodies to the movement protein (MP) of Tobacco mosaic virus: influence of subcellular MP localization and phosphorylation

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