Visualization of the Interaction between the Precursors of VPg, the Viral Protein Linked to the Genome of<i>Turnip Mosaic Virus</i>, and the Translation Eukaryotic Initiation Factor iso 4E In Planta

Beauchemin, Chantal; Boutet, Nathalie; Laliberté, Jean‐François

doi:10.1128/jvi.01277-06

Cited by 150 publications

(129 citation statements)

References 60 publications

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“…interact within virus-induced vesicles (2). Our model, together with the earlier result of trypsin digestion protection of the central helix in vesicle interaction, raises the possibility that a membrane-embedded VPg could still interact with, e.g., eIF4E in the inner leaflet of the vesicle through the central helix.…”

mentioning

confidence: 84%

Structural Flexibility Allows the Functional Diversity of Potyvirus Genome-Linked Protein VPg

Rantalainen

Eskelin

Tompa

et al. 2011

J Virol

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mentioning

confidence: 84%

Structural Flexibility Allows the Functional Diversity of Potyvirus Genome-Linked Protein VPg

Rantalainen

Eskelin

Tompa

et al. 2011

J Virol

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“…Plasmids encoding VPg-Progreen fluorescent protein (GFP), VPg-Pro-DsRed, VPg-Pro-ctGFP, 6K-VPg-Pro-GFP, and ntGFP-eIF(iso)4E were described previously (3) Confocal microscopy. Sections from agroinfiltrated leaves were cut out and placed in immersion oil on a microscope coverglass.…”

Section: Methodsmentioning

confidence: 99%

The Poly(A) Binding Protein Is Internalized in Virus-Induced Vesicles or Redistributed to the Nucleolus during Turnip Mosaic Virus Infection

Beauchemin

Laliberté

2007

J Virol

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Poly(A) binding protein 2 (PABP2) of Arabidopsis thaliana was previously shown to interact with VPg-Pro of turnip mosaic virus (TuMV) and may consequently play an important role during infection. Subcellular fractionation experiments revealed that PABP2 was predominantly a cytoplasmic soluble protein in healthy plants. However, in TuMV-infected plants, a subpopulation of PABP2 was membrane associated or was localized in the nucleus. Confocal microscopy experiments indicated that PABP2 was partially retargeted to the nucleolus in the presence of TuMV VPg-Pro. In addition, the membrane association of PABP2 during TuMV infection resulted from the internalization of the host protein in 6K-VPg-Pro-induced vesicles, as shown by a combination of confocal microscopy and sucrose gradient fractionation experiments. This redistribution of an important translation initiation factor to the nucleolus and to membrane structure likely underlies two important processes of the TuMV replication cycle.Cellular mRNAs are 5Ј capped and 3Ј polyadenylated. The cap structure (m 7 GpppN, where N represents any nucleotide) and the poly(A) tail are involved in translation initiation by interacting with cap-binding eukaryotic initiation factor 4E (eIF4E) and poly(A) binding protein (PABP), respectively. eIF4E is part of the eIF4F complex, which also contains eIF4G and eIF4A. eIF4G functions as a scaffold protein that binds many factors involved in recruiting the 40S ribosomal subunit to mRNAs, among which are eIF4E and PABP (56). The interaction between eIF4G, eIF4E, and PABP and with the

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“…Several potential translational components are associated with RCs of TuMV, including eIF(iso)4E, PABP, eEF1A, and AtRH8 (16)(17)(18)63), but their roles have remained elusive. They may function to regulate viral translation (64), as translation is coupled with replication (35) and RCs (65) during potyvirus infection.…”

Section: Fig 10mentioning

confidence: 99%

“…The model virus of this study, Potato virus A (PVA), is a positive-stranded RNA virus belonging to the genus Potyvirus. Several host proteins that function in translation have been associated with RCs of Turnip mosaic virus (TuMV) (genus Potyvirus), including eIF(iso)4E, PABP, and eEF1A (16)(17)(18). Since both PABP and eEF1A interact with the TuMV RNA-dependent RNA polymerase (RdRp), PABP and eEF1A may function in RNA replication (18,19).…”

mentioning

confidence: 99%

Ribosomal Protein P0 Promotes Potato Virus A Infection and Functions in Viral Translation Together with VPg and eIF(iso)4E

Hafrén

Eskelin

Mäkinen

2013

J Virol

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We report here that the acidic ribosomal protein P0 is a component of the membrane-associated Potato virus A (PVA) ribonucleoprotein complex. As a constituent of the ribosomal stalk, P0 functions in translation. Although the ribosomal stalk proteins P0, P1, P2, and P3 are all important for PVA infection, P0 appears to have a distinct role from those of the other stalk proteins in infection. Our results indicate that P0 also regulates viral RNA functions as an extraribosomal protein. We reported previously that PVA RNA can be targeted by VPg to a specific gene expression pathway that protects the viral RNA from degradation and facilitates its translation. Here, we show that P0 is essential for this activity of VPg, similar to eIF4E/eIF(iso)4E. We also demonstrate that VPg, P0, and eIF(iso)4E synergistically enhance viral translation. Interestingly, the positive effects of VPg and P0 on viral translation were negatively correlated with the cell-to-cell spread of infection, suggesting that these processes may compete for viral RNA.

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Visualization of the Interaction between the Precursors of VPg, the Viral Protein Linked to the Genome ofTurnip Mosaic Virus, and the Translation Eukaryotic Initiation Factor iso 4E In Planta

Cited by 150 publications

References 60 publications

Structural Flexibility Allows the Functional Diversity of Potyvirus Genome-Linked Protein VPg

Structural Flexibility Allows the Functional Diversity of Potyvirus Genome-Linked Protein VPg

The Poly(A) Binding Protein Is Internalized in Virus-Induced Vesicles or Redistributed to the Nucleolus during Turnip Mosaic Virus Infection

Ribosomal Protein P0 Promotes Potato Virus A Infection and Functions in Viral Translation Together with VPg and eIF(iso)4E

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