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与GyrA相互作用的GyrB结构域突变对结核分枝杆菌螺旋酶功能的影响
引用本文:王茂淋,黄友谊,左怀雨,张吉斌.与GyrA相互作用的GyrB结构域突变对结核分枝杆菌螺旋酶功能的影响[J].华中农业大学学报,2017,36(4):71-75.
作者姓名:王茂淋  黄友谊  左怀雨  张吉斌
作者单位:农业微生物学国家重点实验室/华中农业大学生命科学技术学院,武汉,430070
基金项目:国家自然科学基金项目(31070685)
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。

关 键 词:结核分枝杆菌DNA螺旋酶  GyrB缺失突变体  松弛活性  切割活性
收稿时间:2017/1/16 0:00:00

Effects of domain truncated mutant of GyrB interacting with GyrA of DNA gyrase from Mycobacterium tuberculosis on its holoenzymical function
WANG Maolin,HUANG Youyi,ZUO Huaiyu,ZHANG Jibin.Effects of domain truncated mutant of GyrB interacting with GyrA of DNA gyrase from Mycobacterium tuberculosis on its holoenzymical function[J].Journal of Huazhong Agricultural University,2017,36(4):71-75.
Authors:WANG Maolin  HUANG Youyi  ZUO Huaiyu  ZHANG Jibin
Abstract: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.
Keywords:Mycobacterium tuberculosis DNA gyrase  truncated mutants of GyrB  relaxation activity  cleavage activity
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