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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2017.7
- 수록면
- 403 - 410 (8page)
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초록· 키워드
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Background: Prenyltransferases catalyze the sequential addition of isopentenyl diphosphate units to allylic prenyl diphosphate acceptors and are classified as either trans-prenyltransferases (TPTs) or cisprenyltransferases (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 rer2D 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 rer2D via possible protein eprotein interaction with PgCPTL2.
Conclusion: Partial complementation of the yeast dolichol biosynthesis mutant rer2D 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.
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 rer2D 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 rer2D via possible protein eprotein interaction with PgCPTL2.
Conclusion: Partial complementation of the yeast dolichol biosynthesis mutant rer2D 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.
목차
ABSTRACT
1. Introduction
2. Materials and methods
3. Results and discussion
4. Conclusion
References
참고문헌 (32)
참고문헌 신청
[학술지(정기간행물)] - Bach TJ / 1995 / Some new aspects of isoprenoid biosynthesis in plants: a review / Lipids 30 : 191 ~ 202
[학술지(정기간행물)] - Rodíguez-Concepción M / 2002 / Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics / Plant Physiol 130 : 1079 ~ 1089
[학술지(정기간행물)] - Kim YJ / 2014 / Functional analysis of 3-hydroxy-3-methylglutaryl coenzyme a reductase encoding genes in triterpene saponinproducing ginseng / Plant Physiol 165 : 373 ~ 387
[학술지(정기간행물)] - Akhtar TA / 2013 / The tomato cis-prenyltransferase gene family / Plant J 73 : 640 ~ 652
[학술지(정기간행물)] - Liang PH / 2002 / Structure, mechanism, and function of prenyltransferases / Eur J Biochem 269 : 3339 ~ 3354
[학술지(정기간행물)] - Rodíguez-Concepción M / 2002 / Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics / Plant Physiol 130 : 1079 ~ 1089
[학술지(정기간행물)] - Kim YJ / 2014 / Functional analysis of 3-hydroxy-3-methylglutaryl coenzyme a reductase encoding genes in triterpene saponinproducing ginseng / Plant Physiol 165 : 373 ~ 387
[학술지(정기간행물)] - Akhtar TA / 2013 / The tomato cis-prenyltransferase gene family / Plant J 73 : 640 ~ 652
[학술지(정기간행물)] - Liang PH / 2002 / Structure, mechanism, and function of prenyltransferases / Eur J Biochem 269 : 3339 ~ 3354
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UCI(KEPA) : I410-ECN-0101-2018-524-001599135