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近日，學(xué)術(shù)期刊《the Journal of BioLogical Chemistry》在線發(fā)表上海交通大學(xué)微生物代謝國家重點實驗室由德林教授研究組與中國農(nóng)業(yè)科學(xué)院上海獸醫(yī)研究所胡青海課題組合作發(fā)表關(guān)于DNA磷硫?；揎椦芯啃逻M展文章，揭示了DNA解旋酶參與DNA磷硫?；揎椷^程。文章的題目是“DndEi exhibits helicase activity essential for DNA phosphorothioate modification and ATPase activity strongly stimulated by DNA substrate with a GAAC/GTTC motif”，博士生鄭濤為論文*作者。

DNA磷硫?；橇蛟尤〈鶧NA骨架非橋聯(lián)氧原子的一種新型表觀遺傳學(xué)修飾，這種修飾廣泛存在于原核生物中，由磷硫?；揎椈騞ndA-E控制。zui近，來自法國一個研究小組發(fā)現(xiàn)致病微生物Riemerella anatipestifer中存在一種新的DndE蛋白并命名為DndEi。DndEi比傳統(tǒng)的DndE蛋白多1個結(jié)構(gòu)域，但該結(jié)構(gòu)域在DNA磷硫?；揎椫械淖饔蒙胁磺宄?。

本研究通過對R. anatipestifer來源的磷硫?；揎椈駾ndEi生化性質(zhì)和體內(nèi)功能的全面分析，系統(tǒng)闡述了dndEi在DNA磷硫?；揎椫械淖饔?。研究表明DndEi中多出的結(jié)構(gòu)域具有DNA解旋酶活性，體內(nèi)缺失該結(jié)構(gòu)域?qū)е翫NA磷硫?；钚詥适?，證明了該結(jié)構(gòu)域?qū)NA磷硫?；揎検潜匦璧摹Ｑ芯窟€發(fā)現(xiàn)DndEi具有ATP酶活性，并且，含有GAAC/GTTC序列的dna片段能極大的促進DndEi的ATP酶活性，而GAAC/GTTC正是DNA磷硫?；揎椀谋Ｊ匦蛄?。該研究揭示了DNA解旋酶參與DNA磷硫?；揎?，為進一步深入理解DNA磷硫?；纳锘瘜W(xué)過程奠定了重要基礎(chǔ)。

<img alt="JBC:上海交通大學(xué)由德林研究組揭示DNA解旋酶參與DNA磷硫酰化修飾" "="" data-cke-saved-src="http://www.bio1000。。ｃｏｍ/uploads/allimg/151208/1H0561345-0.jpg" src="http://www.bio1000。。ｃｏｍ/uploads/allimg/151208/1H0561345-0.jpg" style="vertical-align: middle; border: 0px; width: 500px; height: 396px;">
原文鏈接：

DndEi exhibits helicase activity essential for DNA phosphorothioate modification and ATPase activity strongly stimulated by DNA substrate with a GAAC/GTTC motif

原文摘要:

Phosphorothioate (PT) modification of DNA, in which the non-bridging oxygen of the backbone phosphate group is replaced by sulfur, is governed by the DndA-E proteins in prokaryotes. To better understand the biochemical mechanism of PT modification, functional analysis of the recently found PT-modifying enzymeDndEi, which has an additional domain compared to canonical DndE, from Riemerella anatipestifer is performed in this study. The additional domain is identified as an ATP-dependent DNA helicase, and functional deletion of this domain in vivo leads to PT modification deficiency, indicating an essential role of helicase activity in PT modification. Subsequent analysis reveals that the additional domain has an ATPase activity. Intriguingly, the ATPase activity is strongly stimulated by DNA substrate containing a GAAC/GTTC motif (i.e., the motif at which PT modifications occur in R. anatipestifer) when the additional domain and the other domain (homologous to canonical DndE) are co-expressed as a full-length DndEi. These results reveal that PT modification is a biochemical process with DNA strands separation and intense ATP hydrolysis.