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Cloning, characterization, and transformation of the phosphoethanolamine N-methyltransferase gene (ZmPEAMT1) in maize (Zea mays L.).
Wu, Suowei; Yu, Zhanwang; Wang, Fengge; Li, Weihua; Ye, Chunjiang; Li, Jun; Tang, Jihua; Ding, Junqiang; Zhao, Jiuran; Wang, Bin.
Afiliação
  • Wu S; The State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.
Mol Biotechnol ; 36(2): 102-12, 2007 Jun.
Article em En | MEDLINE | ID: mdl-17914189
ABSTRACT
N-methylation of phosphoethanolamine, the committing step in choline (Cho) biosynthesis in plants, is catalyzed by S-adenosyl-L-methionine phosphoethanolamine N-methyltransferase (PEAMT, EC 2.1.1.103). Herein we report the cloning and characterization of the novel maize phosphoethanolamine N-methyltransferase gene (ZmPEAMT1) using a combination of bioinformatics and a PCR-based allele mining strategy. The cDNA sequence of ZmPEAMT1 gene is 1,806 bp in length and translates a 495 amino acids peptide. The upstream promoter sequence of ZmPEAMT1 were obtained by TAIL-PCR, and contained four kinds of putative cis-acting regulatory elements, including stress-responsive elements, phytohormone-responsive elements, pollen developmental special activation elements, and light-induced signal transduction elements, as well as several other structural features in common with the promoter of rice and Arabidopsis homologies. RT-PCR analysis showed that expression of ZmPEAMT1 was induced by salt stress and suppressed by high temperature. Over-expression of ZmPEAMT1 enhanced the salt tolerance, root length, and silique number in transgenic Arabidopsis. These data indicated that ZmPEAMT1 maybe involved in maize root development and stress resistance, and maybe having a potential application in maize genetic engineering.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Zea mays / Metiltransferases Idioma: En Revista: Mol Biotechnol Assunto da revista: BIOLOGIA MOLECULAR / BIOTECNOLOGIA Ano de publicação: 2007 Tipo de documento: Article País de afiliação: China
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Zea mays / Metiltransferases Idioma: En Revista: Mol Biotechnol Assunto da revista: BIOLOGIA MOLECULAR / BIOTECNOLOGIA Ano de publicação: 2007 Tipo de documento: Article País de afiliação: China