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heteromeric and Homomeric Geranyl Diphosphate Synthases from Catharanthus roseus and Their Role in Monoterpene Indole Alkaloid Biosynthesis

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Molecular Plant 2013年第5期6卷 1531-1549页

作者： Avanish Rai Shachi S. Smita Anup Kumar Singh Karuna Shanker Dinesh A. Nagegowda CSIR-Central Institute of Medicinal and Aromatic Plants Research Centre Bangalore 560065 India CSIR-Central Institute of Medicinal and Aromatic Plants Lucknow 226015 India

Catharanthus roseus is the sole source of two most important monoterpene indole alkaloid （MIA） anti- cancer agents： vinblastine and vincristine. MIAs possess a terpene and an indole moiety derived from terpenoid and shikimate pathways, respectively. Geranyl diphosphate （GPP）, the entry point to the formation of terpene moiety, is a product of the condensation of isopentenyl diphosphate （IPP） and dimethylallyl diphosphate （DMAPP） by GPP synthase （GPPS）. Here, we report three genes encoding proteins with sequence similarity to large subunit （***） and small subunit （***） of heteromeric GPPSs, and a homomeric GPPSs. *** is a bifunctional enzyme producing both GPP and geranyl geranyl diphosphate （GGPP）, *** is inactive, whereas CrGPPS is a homomeric enzyme forming GPP. Co-expression of both subunits in Escherichia coil resulted in heteromeric enzyme with enhanced activity producing only GPR While *** and CrGPPS showed higher expression in older and younger leaves, respectively, *** showed an increasing trend and decreased gradually. Methyl jasmonate （MelA） treatment of leaves sig- nificantly induced the expression of only ***. GFP localization indicated that *** is plastidial whereas CrGPPS is mitochondrial. Transient overexpression of *** in C. roseus leaves resulted in increased vindoline, immediate monomeric precursor of vinblastine and vincristine. Although C. roseus has both heteromeric and homomeric GPPS enzymes, our results implicate the involvement of only heteromeric GPPS with *** regulating the GPP flux for MIA biosynthesis.

关键词： C. roseus monoterpene indole alkaloids geranyl diphosphate synthase heteromer homomer large subunit small subunit vindoline.

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Fluorescence resonance energy transfer analysis of subunit assembly of the ASIC channel

Fluorescence resonance energy transfer analysis of subunit a...

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中国神经科学学会第四次会员代表大会暨第七届全国学术会议

作者： Ying GAO~1,Shuang-Shuang LIU~1,Shuang QIU~1,Wei CHENG~2,Jie ZHENG~2,Jian-Hong LUO~(1*) 1Department of Neurobiology,Institute for Neuroscience,Zhejiang University School of Medicine,Hangzhou 310058, China 2 Department of Physiology and Membrane Biology,University of California,Davis,School of Medicine,Davis, CA 95616,USA

＜正＞Acid-sensing ion channels（ASICs） are believed to be homo- or heteromeric complexes,which have been verified by classical methods such as co-immunoprecipitation or electrophysiological ***,the exact subunit combinations of ASICs in living cells have not been established ***,we apply assays based on fluorescence resonance energy transfer（FRET） between GFP color mutants CFP and YFP to investigate ASIC assembly directly in living *** as well as heteromerization of different combinations of ASIC subunits were *** addition,our results suggest the formation of heteromeric 1a/2a channels of stoichiometry consisting of at least two la subunits and two 2a *** stoichiometry was observed from heteromeric 1a/2b and 2a/2b *** results imply that these heteromeric ASIC channels contain at least four subunits.

关键词： FRET ASIC assembly homomer heteromer stoichiometry CHO

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