國家衛生研究院 NHRI:Item 3990099045/10908
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 12145/12927 (94%)
造訪人次 : 912241      線上人數 : 1179
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 查詢小技巧：
  • 您可在西文檢索詞彙前後加上"雙引號"，以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋，建議至進階搜尋限定作者欄位，可獲得較完整資料
    •  進階搜尋
    主頁 ‧ 登入 ‧ 上傳 ‧ 說明 ‧ 關於NHRI ‧ 管理 到手機版


    請使用永久網址來引用或連結此文件: http://ir.nhri.org.tw/handle/3990099045/10908


    題名: Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction
    作者: Naik, MT;Kang, M;Ho, CC;Liao, PH;Hsieh, YL;Naik, NM;Wang, SH;Chang, I;Shih, HM;Huang, TH
    貢獻者: Institute of Molecular and Genomic Medicine
    摘要: The negatively charged amino acid-dependent sumoylation motif (NDSM) carries an additional stretch of acidic residues downstream of the consensus psi-K-x-E/D sumoylation motif. We have previously shown that acetylation of the SUMO E2 conjugase enzyme, Ubc9, at K65 downregulates its binding to the NDSM and renders a selective decrease in sumoylation of substrates with the NDSM motif. Here, we provide detailed structural, thermodynamic, and kinetics results of the interactions between Ubc9 and its K65 acetylated variant (Ac-Ubc9(K65)) with three NDSMs derived from Elk1, CBP, and Calpain2 to rationalize the mechanism beneath this reduced binding. Our nuclear magnetic resonance (NMR) data rule out a direct interaction between the NDSM and the K65 residue of Ubc9. Similarly, we found that NDSM binding was entropy-driven and unlikely to be affected by the negative charge by K65 acetylation. Moreover our NMR, mutagenesis and molecular dynamics simulation studies defined the sequence of the NDSM as psi-K-x-E/D-x(1)-x(2)-(x(3)/E/D)-(x(4)/E/D)-x(n) and determined that K74 and K76 were critical Ubc9 residues interacting with the negatively charged residues of the NDSM.
    日期: 2017-12
    關聯: Scientific Reports. 2017 Dec;7:Article number 17391.
    Link to: http://dx.doi.org/10.1038/s41598-017-17465-0
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2045-2322&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000417689400015
    Cited Times(Scopus): https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85037722627
    顯示於類別:[施修明] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    ISI000417689400015.pdf3144KbAdobe PDF380檢視/開啟


    在NHRI中所有的資料項目都受到原著作權保護.

    TAIR相關文章

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