C-terminal hydrophobic region leads PRSV P3 protein to endoplasmic reticulum
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P3 protein is one of the least characterized potyviral proteins in both functions and sub-cellular localization. In this study, we examined the sub-cellular localization of PRSV P3 and its intermediate, P3-6K1 by expressing their GFP fusion proteins in onion epidermal cells. Our results showed that both P3- and P3-6K1 GFP fusion proteins were localized at the endoplasmic reticulum. Deletion analysis indicated that C-terminal of P3 protein contained localization signal, and a 19 amino acids hydrophobic domain from this region was able to target the GFP fusion protein to endoplasmic reticulum. C-terminal of P3 proteins has been suggested to be involved in both viability and pathogenicity of the potyvirus. Therefore, our result suggests that localization of P3 protein at endoplasmic reticulum is essential for functionality of P3 protein.
KeywordsPotyvirus P3 Localization Hydrophobic Endoplasmic Reticulum PRSV
We thank Dr. Kusol Pootanakit and Professor Sakol Panyim, IMBG, Mahidol University for valuable discussion and critical reading of the manuscript; Mr. Sarun Kunwittaya, NICFD, Mahidol University for technical advice to operate the fluorescent microscope; Dr. Scott G. Franzblau, University of Illinois and the Flanders Interuniversity Institute of Biotechnology (VIB), Ghent University, Belgium for the kind gift of pDsRed2 and pKar6-gfp plasmids respectively. S.E is the recipient of Mahidol University Medical scholar Program (PhD-MD). This study was supported by the Mahidol University Research Grant, “RNA Interference for Plant Virus Resistance” and TRF grant MRG4980038.