古菌Hef蛋白解旋酶结构域与核酸酶结构域之间内在无序区域的多重相互作用。
Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein.
作者信息
Ishino Sonoko, Yamagami Takeshi, Kitamura Makoto, Kodera Noriyuki, Mori Tetsuya, Sugiyama Shyogo, Ando Toshio, Goda Natsuko, Tenno Takeshi, Hiroaki Hidekazu, Ishino Yoshizumi
机构信息
From the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, and Faculty of Agriculture, Kyushu University, Fukuoka 812-8581.
the Bio-AFM Frontier Research Center and Department of Physics, College of Science and Engineering, Kanazawa University, Kanazawa 920-1192, and.
出版信息
J Biol Chem. 2014 Aug 1;289(31):21627-39. doi: 10.1074/jbc.M114.554998. Epub 2014 Jun 19.
Hef is an archaeal protein that probably functions mainly in stalled replication fork repair. The presence of an unstructured region was predicted between the two distinct domains of the Hef protein. We analyzed the interdomain region of Thermococcus kodakarensis Hef and demonstrated its disordered structure by CD, NMR, and high speed atomic force microscopy (AFM). To investigate the functions of this intrinsically disordered region (IDR), we screened for proteins interacting with the IDR of Hef by a yeast two-hybrid method, and 10 candidate proteins were obtained. We found that PCNA1 and a RecJ-like protein specifically bind to the IDR in vitro. These results suggested that the Hef protein interacts with several different proteins that work together in the pathways downstream from stalled replication fork repair by converting the IDR structure depending on the partner protein.
Hef是一种古菌蛋白，其主要功能可能是参与停滞复制叉的修复。据预测，Hef蛋白的两个不同结构域之间存在一个无结构区域。我们分析了嗜热栖热菌Hef的结构域间区域，并通过圆二色光谱（CD）、核磁共振（NMR）和高速原子力显微镜（AFM）证实了其无序结构。为了研究这个内在无序区域（IDR）的功能，我们通过酵母双杂交方法筛选与Hef的IDR相互作用的蛋白质，获得了10种候选蛋白质。我们发现PCNA1和一种类RecJ蛋白在体外能特异性结合IDR。这些结果表明，Hef蛋白通过根据伴侣蛋白改变IDR结构，与几种不同的蛋白质相互作用，这些蛋白质在停滞复制叉修复的下游通路中协同发挥作用。
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