Please use this identifier to cite or link to this item: https://doi.org/10.1094/MPMI-22-12-1523
Title: Plastocyanin transit peptide interacts with Potato virus X coat protein, while silencing of plastocyanin reduces coat protein accumulation in chloroplasts and symptom severity in host plants
Authors: Qiao, Y.
Li, H.F.
Wong, S.M. 
Fan, Z.F.
Issue Date: Dec-2009
Citation: Qiao, Y., Li, H.F., Wong, S.M., Fan, Z.F. (2009-12). Plastocyanin transit peptide interacts with Potato virus X coat protein, while silencing of plastocyanin reduces coat protein accumulation in chloroplasts and symptom severity in host plants. Molecular Plant-Microbe Interactions 22 (12) : 1523-1534. ScholarBank@NUS Repository. https://doi.org/10.1094/MPMI-22-12-1523
Abstract: Potato virus X coat protein (PVXCP) is, through communication with host proteins, involved in processes such as virus movement and symptom development. Here, we report that PVXCP also interacts with the precursor of plastocyanin, a protein involved in photosynthesis, both in vitro and in vivo. Yeast two-hybrid analysis indicated that PVXCP interacted with only the plastocyanin transit peptide. In subsequent bimolecular fluorescence complementation assays, both proteins were collocated within chloroplasts. Western blot analyses of chloroplast fractions showed that PVXCP could be detected in the envelope, stroma, and lumen fractions. Transmission electron microscopy demonstrated that grana were dilated in PVX-infected Nicotiana benthamiana. Furthermore, virus-induced gene silencing of plastocyanin by prior infection of N. benthamiana using a Tobacco rattle virus vector reduced the severity of symptoms that developed following subsequent PVX infection as well as the accumulation of PVXCP in isolated chloroplasts. However, PVXCP could not be detected in pea chloroplasts in an in vitro re-uptake assay using the plastocyanin precursor protein. Taken together, these data suggest that PVXCP interacts with the plastocyanin precursor protein and that silencing the expression of this protein leads to reduced PVXCP accumulation in chloroplasts and ameliorates symptom severity in host plants. © 2009 The American Phytopathological Society.
Source Title: Molecular Plant-Microbe Interactions
URI: http://scholarbank.nus.edu.sg/handle/10635/101416
ISSN: 08940282
DOI: 10.1094/MPMI-22-12-1523
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