Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity.

Crum, Carol; Hu, Jie; Hiddinga, H J; Roth, Don A.

doi:10.1016/s0021-9258(18)37724-x

Cited by 36 publications

(2 citation statements)

References 25 publications

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“…Phosphorylation of eIF2α in plants does not apparently shut off protein synthesis similarly to that described in mammalian cell culture (Hu and Roth, unpublished results). Further, increased pPKR phosphorylation following plant virus infection does not appear to have antiviral consequences ( , ). The physiological significance of plant eIF2α phosphorylation in planta has not been demonstrated, although differential eIF2α phosphorylation has been shown during plant development ( , ).…”

Section: Discussionmentioning

confidence: 99%

“…In vitro phosphorylation of the M r 68 000 pPKR is stimulated by dsRNA, select polyanions, or intramolecularly base-paired, single-stranded RNAs of sufficient length but not by DNA or RNA-DNA hybrids (24). Similarly to mammalian PKR (18), autophosphorylation is inhibited by high levels of dsRNA (23,25). Both pPKR and mammalian PKR are localized in the † The assistance of the Ministry of Education and Culture of Spain, SAB1998-01444 that supported the sabbatical leave of D.R.…”

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confidence: 99%

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In Vivo Regulation of Protein Synthesis by Phosphorylation of the α Subunit of Wheat Eukaryotic Initiation Factor 2

2000

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The regulation of protein synthesis is a critical component in the maintenance of cellular homeostasis. A major mechanism of translational control in response to diverse abiotic and biotic stress signals involves the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha). The pathway has been demonstrated in all eukaryotes except plants, although components of a putative plant pathway have been characterized. To evaluate the in vivo capability of plant eIF2alpha to participate in the translation pathway, we have used vaccinia virus recombinants that constitutively express wheat eIF2alpha and inducibly express the eIF2alpha dsRNA-stimulated protein kinase, PKR, in BSC-40 cells. Activation of PKR in cells expressing wild-type wheat eIF2alpha resulted in an inhibition of cellular and viral protein synthesis and an induction of cellular apoptosis correlating with phosphorylation of eIF2alpha on serine 51. Expression of a nonphosphorylatable mutant (51A) of plant eIF2alpha reversed the PKR-mediated translational block as well as the PKR-induced apoptosis. A direct interaction of the plant proteins with the mammalian translational initiation apparatus is supported by coimmunoprecipitation of wild-type plant eIF2alpha and the 51A mutant with mammalian eIF2gamma and the localization of the plant proteins in ribosome fractions. These findings suggest that plant eIF2alpha is capable of interacting with the guanine nucleotide exchange factor eIF2B within the context of the eIF2 holoenzyme and provide direct evidence for its ability to participate in phosphorylation-mediated translational control in vivo.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

In Vivo Regulation of Protein Synthesis by Phosphorylation of the α Subunit of Wheat Eukaryotic Initiation Factor 2

2000

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Virus-Induced Host Gene Shutoff in Animals and Plants

Aranda

Maule

1998

Virology

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The Cauliflower Mosaic Virus Translational Transactivator Interacts with the 60S Ribosomal Subunit Protein L18 of Arabidopsis thaliana

2000

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The cauliflower mosaic virus (CaMV) open reading frame VI product (P6) is involved in several aspects of the infectious cycle. P6 specifically controls the synthesis of other CaMV proteins by transactivating their expression from the polycistronic 35S RNA. By far-Western assays, we have demonstrated that P6 interacts with proteins from both healthy and CaMV-infected leaves of Arabidopsis thaliana. These proteins are found in ribosome-enriched extracts, suggesting that they participate in the translation process. One of these proteins, identified by microsequencing, corresponds to the 60S ribosomal subunit protein L18 (RPL18). Its cDNA was cloned and expressed in Escherichia coli, and the resulting RPL18 protein was shown to interact with the minimal region required for translational transactivation, designated the miniTAV domain of P6.

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Tobacco mosaic virus infection stimulates the phosphorylation of a plant protein associated with double-stranded RNA-dependent protein kinase activity.

Cited by 36 publications

References 25 publications

In Vivo Regulation of Protein Synthesis by Phosphorylation of the α Subunit of Wheat Eukaryotic Initiation Factor 2

In Vivo Regulation of Protein Synthesis by Phosphorylation of the α Subunit of Wheat Eukaryotic Initiation Factor 2

Virus-Induced Host Gene Shutoff in Animals and Plants

The Cauliflower Mosaic Virus Translational Transactivator Interacts with the 60S Ribosomal Subunit Protein L18 of Arabidopsis thaliana

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