國家衛生研究院 NHRI:Item 3990099045/7854
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    题名: Structural basis for DNA-mediated allosteric regulation facilitated by the AAA(+) module of Lon protease
    作者: Lee, AY;Chen, YD;Chang, YY;Lin, YC;Chang, CF;Huang, SJ;Wu, SH;Hsu, CH
    贡献者: National Institute of Cancer Research
    摘要: Lon belongs to a unique group of AAA(+) proteases that bind DNA. However, the DNA-mediated regulation of Lon remains elusive. Here, the crystal structure of the alpha subdomain of the Lon protease from Brevibacillus thermoruber (Bt-Lon) is presented, together with biochemical data, and the DNA-binding mode is delineated, showing that Arg518, Arg557 and Arg566 play a crucial role in DNA binding. Electrostatic interactions contributed by arginine residues in the AAA(+) module are suggested to be important to DNA binding and allosteric regulation of enzymatic activities. Intriguingly, Arg557, which directly binds DNA in the alpha subdomain, has a dual role in the negative regulation of ATPase stimulation by DNA and in the domain-domain communication in allosteric regulation of Bt-Lon by substrate. In conclusion, structural and biochemical evidence is provided to show that electrostatic interaction in the AAA(+) module is important for DNA binding by Lon and allosteric regulation of its enzymatic activities by DNA and substrate.
    日期: 2014-02
    關聯: Acta Crystallographica. Section D, Biological Crystallography. 2014 Feb;70(Pt 2):218-230.
    Link to: http://dx.doi.org/10.1107/s139900471302631x
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2059-7983&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000331554500002
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84894179110
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