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http://dx.doi.org/10.1016/j.jgr.2017.01.013

cis-Prenyltransferase interacts with a Nogo-B receptor homolog for dolichol biosynthesis in Panax ginseng Meyer  

Nguyen, Ngoc Quy (Department of Plant Biotechnology, College of Agriculture and Life Science, Chonnam National University)
Lee, Sang-Choon (Department of Plant Science, Plant Genomics and Breeding Institute, College of Agriculture and Life Sciences, Seoul National University)
Yang, Tae-Jin (Department of Plant Science, Plant Genomics and Breeding Institute, College of Agriculture and Life Sciences, Seoul National University)
Lee, Ok Ran (Department of Plant Biotechnology, College of Agriculture and Life Science, Chonnam National University)
Publication Information
Journal of Ginseng Research / v.41, no.3, 2017 , pp. 403-410 More about this Journal
Abstract
Background: Prenyltransferases catalyze the sequential addition of isopentenyl diphosphate units to allylic prenyl diphosphate acceptors and are classified as either trans-prenyltransferases (TPTs) or cis-prenyltransferases (CPTs). The functions of CPTs have been well characterized in bacteria, yeast, and mammals compared to plants. The characterization of CPTs also has been less studied than TPTs. In the present study, molecular cloning and functional characterization of a CPT from a medicinal plant, Panax ginseng Mayer were addressed. Methods: Gene expression patterns of PgCPT1 were analyzed by quantitative reverse transcription polymerase chain reaction. In planta transformation was generated by floral dipping using Agrobacterium tumefaciens. Yeast transformation was performed by lithium acetate and heat-shock for $rer2{\Delta}$ complementation and yeast-two-hybrid assay. Results: The ginseng genome contains at least one family of three putative CPT genes. PgCPT1 is expressed in all organs, but more predominantly in the leaves. Overexpression of PgCPT1 did not show any plant growth defect, and its protein can complement yeast mutant $rer2{\Delta}$ via possible protein-protein interaction with PgCPTL2. Conclusion: Partial complementation of the yeast dolichol biosynthesis mutant $rer2{\Delta}$ suggested that PgCPT1 is involved in dolichol biosynthesis. Direct protein interaction between PgCPT1 and a human Nogo-B receptor homolog suggests that PgCPT1 requires an accessory component for proper function.
Keywords
cis-prenyltransferases; dolichol; Nogo-B receptor; Panax ginseng; polyisoprenoid;
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