國家衛生研究院 NHRI:Item 3990099045/7854
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 12145/12927 (94%)
Visitors : 855694      Online Users : 1327
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
    •  Adv. Search
    Home ‧ Login ‧ Upload ‧ Help ‧ About ‧ Administer Goto mobile version


    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/7854


    Title: Structural basis for DNA-mediated allosteric regulation facilitated by the AAA(+) module of Lon protease
    Authors: Lee, AY;Chen, YD;Chang, YY;Lin, YC;Chang, CF;Huang, SJ;Wu, SH;Hsu, CH
    Contributors: National Institute of Cancer Research
    Abstract: 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.
    Date: 2014-02
    Relation: 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
    Appears in Collections:[Alan Yueh-Luen Lee] Periodical Articles

    Files in This Item:

    File Description SizeFormat
    PUB24531457.pdf1339KbAdobe PDF578View/Open


    All items in NHRI are protected by copyright, with all rights reserved.

    Related Items in TAIR

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback