详细信息
ChIP-seq and structural analyses delineating the regulatory mechanism of master regulator EsrB in Edwardsiella piscicida ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:ChIP-seq and structural analyses delineating the regulatory mechanism of master regulator EsrB in Edwardsiella piscicida
作者:Zhang, Boya[1];Zhang, Yi[1];Liu, Jingjing[2];Reverter, David[3];Wang, Qiyao[1,4];Choi, Sang Ho[5];Liu, Bing[2];Shao, Shuai[1,4]
机构:[1]East China Univ Sci & Technol, Shanghai Frontiers Sci Ctr Optogenet Tech Cell Met, State Key Lab Bioreactor Engn, Shanghai, Peoples R China;[2]Hangzhou Normal Univ, Sch Basic Med Sci, Dept Biochem & Mol Biol, Hangzhou, Peoples R China;[3]Univ Autonoma Barcelona, Inst Biotecnol & Biomed IBB, Barcelona, Spain;[4]Engn Res Ctr Maricultured Anim Vaccines, Shanghai, Peoples R China;[5]Seoul Natl Univ, Dept Agr Biotechnol, Natl Res Lab Mol Microbiol & Toxicol, Seoul, South Korea
年份:2024
卷号:90
期号:12
外文期刊名:APPLIED AND ENVIRONMENTAL MICROBIOLOGY
收录:;EI(收录号:20245217573047);WOS:【SCI-EXPANDED(收录号:WOS:001355861500001)】;
基金:MOST | National Key Research and Development Program of China (NKPs) 2022YFE0101200 Qiyao Wang.MOST | National Natural Science Foundation of China (NSFC) 32373183 Shuai Shao.China Agriculture Research System of MOF and MARA CARS-47 Qiyao WangMinisterio de Ciencia e Innovacion (MCIN) PID2021-124602OB-100 David Reverter.
语种:英文
外文关键词:ChIP-seq; crystal structure; Edwardsiella piscicida; EsrB; metabolism; pathogenesis
摘要:As a response regulator of the EsrA-EsrB two-component system, EsrB is conserved in Hafniaceae and plays a crucial role in virulence and pathogenicity. EsrB possesses DNA binding abilities, enabling it to regulate the transcription of virulence genes to confront different stresses and achieve systematic infections. Here, ChIP-seq analysis of EsrB in Dulbecco's Modified Eagle's Medium (DMEM) (mimicking in vivo environments) revealed that EsrB preferred to bind to virulence-associated promoters with a distinct 7'-4-7" pseudopalindromic DNA motif and interact with metabolic-related promoters with a high AT DNA motif. The crystal structure of the C-terminal of EsrB (EsrB(C)) was solved at 2.20-& Aring; resolution. Specifically, Lys(181) enabled the DNA-binding affinity of EsrB and promoted the in vitro and in vivo pathogenicity of Edwardsiella piscicida. Moreover, EsrB directly regulated the expression of genes associated with basal metabolism, including iron and tricarboxylic acid (TCA) cycles. Furthermore, EsrB enhanced iron transport capability and the enzyme activity of succinate dehydrogenase and pyruvate dehydrogenase in DMEM. Collectively, our structural and ChIP-seq analysis provides valuable insights into the DNA binding mechanism of EsrB which will facilitate our understanding of EsrB coordinating virulence and basal metabolism gene expression.
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