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Received November 15, 2012
Accepted April 20, 2013
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Expression characteristics of the maeA and maeB genes by extracellular malate and pyruvate in Escherichia coli

Department of Chemical Engineering, University of Ulsan, 93, Daehak-ro, Nam-gu, Ulsan 680-749, Korea 1Department of Pharmaceutical Science and Technology, Catholic University of Daegu, 330, Geumrak 1-ri, Hayang-eup, Gyeongsan-si, Gyeongbuk 712-702, Korea 2Department of Environmental Engineering and Energy, Myongji University, San 38-2, Nam-dong, Cheoin-gu, Yongin-si, Gyeonggido 449-728, Korea 3Chemical Biotechnology Research Center, Korea Research Institute of Chemical Technology, Yuseong-gu, Daejeon 305-600, Korea
shhong@ulsan.ac.kr
Korean Journal of Chemical Engineering, July 2013, 30(7), 1443-1447(5), 10.1007/s11814-013-0061-4
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Abstract

The malate-pyruvate conversion pathway is catalyzed by two malic enzyme isomers, MaeA and MaeB. qRT-PCR was carried out under malate and pyruvate supplemented conditions to understand the dynamics of maeA and maeB gene expression. maeA expression was elevated by malate, and maeB expression was inhibited by levels of both malate and pyruvate higher than 0.1 mM. Green fluorescent protein (GFP) reporter plasmids were also constructed by integration of the maeA/maeB promoter with the gfp gene. We showed that maeA driven GFP expression_x000D_ was positively and negatively correlated with extracellular malate and pyruvate induction. In contrast, no significant changes in maeB driven GFP expression were observed under both malate and pyruvate supplemented conditions.

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