HMG盒蛋白以其开放构象与四链DNA连接点结合。
HMG box proteins bind to four-way DNA junctions in their open conformation.
作者信息
P-ohler J R, Norman D G, Bramham J, Bianchi M E, Lilley D M
机构信息
CRC Nucleic Acid Structure Research Group, Department of Biochemistry, The University of Dundee, Dundee DD1 4HN, UK.
出版信息
EMBO J. 1998 Feb 2;17(3):817-26. doi: 10.1093/emboj/17.3.817.
Abstract
The HMG box is an 80 amino acid domain found in a variety of eukaryotic chromosomal proteins and transcription factors. Binding to DNA is associated with recognition of structural distortion or manipulation of DNA structure. All the HMG box domains bind to four-way DNA junctions, which must therefore present some feature that is common to the binding targets of this wide variety of proteins. Since the four-way junction can itself adopt a variety of structures depending upon conditions, it is important to determine in which form it exists in complexes with HMG boxes. We find that a single HMG box domain is bound exclusively to the open square form of the junction and that conditions that stabilize the stacked X structure significantly lower affinity for the HMG box. We suggest that the HMG domain binds to one arm of the junction in the minor groove at the point of strand exchange and we present a model for the structure of the complex.
摘要
HMG框是一个由80个氨基酸组成的结构域，存在于多种真核染色体蛋白和转录因子中。与DNA结合与识别结构畸变或操纵DNA结构有关。所有HMG框结构域都与四链DNA连接点结合，因此四链DNA连接点必定呈现出这类多种蛋白质结合靶点所共有的某些特征。由于四链连接点本身可根据条件采用多种结构，因此确定它与HMG框形成复合物时以何种形式存在很重要。我们发现单个HMG框结构域仅与连接点的开放方形形式结合，而稳定堆叠X结构的条件会显著降低对HMG框的亲和力。我们认为HMG结构域在链交换点的小沟中与连接点的一个臂结合，并提出了复合物结构的模型。
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