The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro
The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro
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DOI：
10.1016/j.febslet.2009.03.003
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发表时间：
2009-04-02
期刊：
影响因子：
3.5
通讯作者：
Faraone-Mennella, Maria Rosaria
中科院分区：
文献类型：
--
作者：
Castellano, Sabrina;Farina, Benedetta;Faraone-Mennella, Maria Rosaria
7 kDa Sso 7是一种碱性蛋白，在硫磺硫化叶菌中特别丰富，并参与DNA组装。这种蛋白质通过内源性聚（ADP-核糖）聚合酶样酶进行体外ADP-核糖基化。纯化的ADP-核糖基化的Sso 7的圆二色性光谱表明，该modi。阳离子稳定了普遍的蛋白质β-构象，如负椭圆率最小值移动到220 nm所示。此外，一个短的ADP-核糖链（最多6聚体）绑定到Sso 7是能够大幅降低的热保护和DNA凝聚能力的蛋白质，这表明可能的调节作用的ADP-核糖基化在sulfolobal DNA组织。(C)2009年欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows that this modi. cation stabilizes the prevalent protein beta-conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.