摘要
DNA螺旋酶中的GyrA与GyrB亚基只有互作重组后才有酶活性。为寻找GyrB亚基和GyrA亚基相互作用的关键区域,构建了不同的GyrB亚基突变体,分析GyrB各突变体与GyrA亚基的相互作用对全酶活性的影响。结果显示:GyrB亚基C端是其与GyrA相互作用的主要结构域,结合GyrB的二维结构,提出GyrB中第531~550位氨基酸是影响螺旋酶功能的关键区域,并可能是理想的新药设计靶标。
DNA gyrase has no activity before subunits of GyrA and GyrB recombine to a tetrameric holoenzyme.A series of GyrB mutants has been constructed and the enzymatic activity of these GyrB mutants was analyzed to study the interaction domains of GyrB and GyrA subunits.Results showed that the C-terminus of GyrB subunit is the key domain to interact with GyrA subunit.Combined with analyzing GyrB dimensional structure, 531-550 aa of GyrB was proposed to be the key domain of controlling enzymical activity of DNA gyrase and an ideal target for designing drug.
出处
《华中农业大学学报》
CAS
CSCD
北大核心
2017年第4期71-75,共5页
Journal of Huazhong Agricultural University
基金
国家自然科学基金项目(31070685)
