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Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli.

Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Research Abstract Details 

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  • Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Abstract Text:

    qian wangQian Wang,yan piYan Pi,rong houRong Hou,keji jiangKeji Jiang,zhuoshi huangZhuoshi Huang,ming-shiun hsiehMing-Shiun Hsieh,xiaofen sunXiaofen Sun,kexuan tangKexuan Tang,

    Camptothecin is an anti-cancer monoterpene indole alkaloid. The gene encoding 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (designated as CaHDR), the last catalytic enzyme of the MEP pathway for terpenoid biosynthesis, was isolated from camptothecin-producing Camptotheca acuminata. The full-length cDNA of CaHDR was 1686 bp encoding 459 amino acids. Comparison of the cDNA and genomic DNA of CaHDR revealed that there was no intron in genomic CaHDR. Southern blot analysis indicated that CaHDR belonged to a low-copy gene family. RT-PCR analysis revealed that CaHDR expressed constitutively in all tested plant organs with the highest expression level in flowers, and the expression of CaHDR could be induced by 100 muM methyl-jasmonate (MeJA), but not by 100 mg/L salicylic acid (SA) in the callus of C. acuminata. The complementation of CaHDR in Escherichia coli ispH mutant MG1655 demonstrated its function. [BMB reports 2008; 41(2): 112-118].

    Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Publishing Authors By Initials

    q wangQ Wang,y piY Pi,r houR Hou,k jiangK Jiang,z huangZ Huang,ms hsiehMS Hsieh,x sunX Sun,k tangK Tang,

    For similar abstracts research abstracts see: abstracts research

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    Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: BMB reports

    VOLUME: 41

    Page Numbers: 112-8

    Journal Abbreviation:

    ISSN: 1976-6696

    DAY: 4

    MONTH: Feb

    YEAR: 2008

    Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Information

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    LANGUAGE: eng

    NlmUniqueID: 101465334

    Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Keywords Mesh Terms:

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    Chemical & Substance for Abstract: Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli. Information

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    Grant and Affiliation Information for Molecular cloning and characterization of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase (CaHDR) from Camptotheca acuminata and its functional identification in Escherichia coli.

    AFFILIATION: State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center,Morgan-Tan International Center for Life Sciences, Fudan University, Shanghai, People's Republic of China kxtang1@yahoo.com.

    Country: Korea (South)

    Korea (South) Research PublicationKorea (South) Research Publication

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    MEDLINETA: BMB Rep

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    Molecular cloning and characterization of 1-hydroxy-2-methyl-2-E-butenyl 4-diphosphate reductase CaHDR from Camptotheca acuminata and its functional identification in Escherichia coli Related Publications

     

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