ArticleProtoplasma2011
Subcellular localization of V2 protein of Tomato leaf curl Java virus by using green fluorescent protein and yeast hybrid system.
Article in Protoplasma, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- RepA Promotes the Nucleolar Exclusion of the V2 Protein of Mulberry Mosaic Dwarf-Associated Virus.Frontiers in microbiology · 2020Article
- Convergent starvation signals and hormone crosstalk in regulating nutrient mobilization upon germination in cereals.The Plant cell · 2012Article
- Functional characterization of coat protein and V2 involved in cell to cell movement of Cotton leaf curl Kokhran virus-Dabawali.PloS one · 2011Article
- Insights Into Virus-Encoded RNA Silencing Suppressors Across Viral Families: A Focus on Viruses Infecting Solanaceae Crops.Physiologia plantarumReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tomato leaf curl Java virus-A (ToLCJV-A[ID]) from Southeast Asia is a new member of the emerging group of monopartite begomoviruses that require a betasatellite component for symptom induction. Previously, we have elucidated the role of V1 ORF encoded by ToLCJV-A[ID] in cell-to-cell movement. In this study, the role of V2 (PreCP) in localization was determined. Subcellular localization of ToLCJV-A[ID] V2 in plant tissues showed that this protein is co-localized to the cell cytoplasm, perinuclear and associated with the endoplasmic reticulum network. The results obtained from deletion analysis indicate that fusion of N-terminal part of the V2, containing the nuclear export signals (NES), directed the accumulation of fluorescence towards the cell cytoplasm. Furthermore, functionality of the NES ((20)LAVKYLQLV(29)) in the N-terminal part of the V2 protein was confirmed by one-hybrid yeast system. Taken together, these results suggest that V2 enhances the coat protein-mediated nuclear export of ToLCJV-A[ID] and is consistent with the model in which V2 mediates viral DNA export from the nucleus to the plasmodesmata.
Indexed as
Identifiers
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Registered trials
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