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Research Notes · Open access · Published 13 June 2015

Subcellular Localization Studies of Three Phenylalanine Ammonia-Lyases and Cinnamate 4-Hydroxylase from Scutellaria Baicalensis Using GFP Fusion Proteins

Nam Il Park1, Hui Xu2, Mariadhas Valan Arasu3, Naif Abdullah Al-Dhabi3 & Sang Un Park4

OnLine Journal of Biological Sciences, Volume 15, Issue 2, pp. 70–73 · doi.org/10.3844/ojbsci.2015.70.73

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Abstract

The localization of three phenylalanine ammonia-lyases (PAL1, -2 and -3) and Cinnamate 4-Hydroxlase (C4H) of Scutellaria baicalensis was examined in onion epidermal cells. These genes encode key enzymes in the phenylpropanoid pathway for the synthesis of flavones. In our previous research, we isolated coding DNA for these genes from S. baicalensis, a medicinal herb rich in flavones with biological and pharmacological properties. We observed that SbPAL2, SbPAL3 and SbC4H proteins localize to the endoplasmic reticulum; however, SbPAL1 was a cytosolic protein. Unlike SbPAL2 and SbPAL3, SbPAL1 may be expected to have a different function in the flavone biosynthetic pathway.

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Park, N. I., Xu, H., Arasu, M. V., Al-Dhabi, N. A. & Park, S. U. (2015). Subcellular Localization Studies of Three Phenylalanine Ammonia-Lyases and Cinnamate 4-Hydroxylase from Scutellaria Baicalensis Using GFP Fusion Proteins. OnLine Journal of Biological Sciences, 15(2), 70–73. https://doi.org/10.3844/ojbsci.2015.70.73

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Subcellular Localization Studies of Three Phenylalanine Ammonia-Lyases and Cinnamate 4-Hydroxylase from Scutellaria Baicalensis Using GFP Fusion ProteinsOnLine Journal of Biological Sciences · Volume 15, Issue 2 · pp. 70–73 · CC BY 3.0Download