molecular evolution of threonine dehydratase in bacteria细菌中的苏氨酸脱水酶的分子进化精品.pdfVIP

Molecular Evolution of Threonine Dehydratase in Bacteria 1,2 2 1,3 Xuefei Yu , Ye Li , Xiaoyuan Wang * 1 State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China, 2 Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi, China, 3 Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, China Abstract Threonine dehydratase converts L-threonine to 2-ketobutyrate. Several threonine dehydratases exist in bacteria, but their origins and evolutionary pathway are unknown. Here we analyzed all the available threonine dehydratases in bacteria and proposed an evolutionary pathway leading to the genes encoding three different threonine dehydratases CTD, BTD1 and BTD2. The ancestral threonine dehydratase might contain only a catalytic domain, but one or two ACT-like subdomains were fused during the evolution, resulting BTD1 and BTD2, respectively. Horizontal gene transfer, gene fusion, gene duplication, and gene deletion may occur during the evolution of this enzyme. The results are important for understanding the functions of various threonine dehydratases found in bacteria. Citation: Yu X, Li Y, Wang X (2013) Molecular Evolution of Threonine Dehydratase in Bacteria. PLoS ONE 8(12): e80750. doi:10.1371/journal.pone.0080750 Editor: Dongsheng Zhou, Beijing Institute of Microbiology and Epidemiology, China Received July 23, 2013; Accepted October 6, 2013; Published December 4, 2013 Copyright: 2013 Yu et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: This work was financially supported by grants from National