國家衛生研究院 NHRI:Item 3990099045/10908
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    题名: 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
    贡献者: 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
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