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Updated: Jul 14, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
C-terminal hydrophobic region leads PRSV P3 protein to endoplasmic reticulum
Sarasate Eiamtanasate1, Mila Juricek, Yun-Kiam Yap
1Institute of Molecular Biology and Genetics, Mahidol University, Salaya campus, 25/25 Phuttamonthon 4 Road, Salaya, Phuttamonthon, Nakhon Pathom 73170, Thailand.
Abstract:
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.
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