Chinese Bulletin of Botany ›› 2015, Vol. 50 ›› Issue (3): 295-309.DOI: 10.3724/SP.J.1259.2015.00295

• EXPERIMENTAL COMMUNICATIONS • Previous Articles     Next Articles

Analysis of Molecular Evolution and Gene Structure of EPSPS Protein in Plant Shikimate Pathway

Yuanyong Gong1, Shuqiao Guo1, Hongmei Shu1, Wanchao Ni1, *, Paerhati·Maimaiti2, Xinlian Shen1, Peng Xu1, Xianggui Zhang1, Qi Guo1   

  1. 1Institute of Industrial Crops, Jiangsu Academy of Agricultural Sciences/Key Laboratory of Cotton and Rapeseed in the Lower Reaches of Yangtze River, Ministry of Agriculture, Nanjing 210014, China;
    2.National Engineering Techanical Research Center of Cotton, Urumqi 830091, China
  • Received:2014-05-05 Revised:2014-08-28 Online:2015-05-01 Published:2015-04-08

Abstract: 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), a key enzyme with a role in the shikimate pathway of aromatic amino acid biosynthesis in nearly all plants, bacteria, and fungi, is a target enzyme of the herbicide glyphosate [N-(phosphonomethyl) glycine]. The cloning of EPSPS genes can provide candidate gene for the development of glyphosate resistant transgenic crops. Comparative genomic analysis was used to investigate the evolutionary relationship among 43 EPSPS genes in 41 different plant species. The main results are as follows. (1) Various plant EPSPS protein sequences have the same functional domain, conserved motifs and conserved site. However, chloroplast transit peptide sequences significantly differ. (2) Phylogenetic analyses suggested that EPSPS genes correspond to two main branches according to dicotyledoneae and monocotyledoneae, and each small branch was classified based on species kinship of plants. (3) Exon-intron structure analysis revealed that the gene structures of EPSPS basically contained 8 exons and 7 introns, with only a marginal difference in corresponding exons but marked differences in all introns. The change in intron length was the main contributor to the structural diversity of plant EPSPS genes. This study provides valuable information for research into EPSPS proteins in plants.

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