THAP结构域：一种与P因子转座酶的DNA结合结构域相似的新型蛋白质基序。
The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase.
作者信息
Roussigne Myriam, Kossida Sophia, Lavigne Anne-Claire, Clouaire Thomas, Ecochard Vincent, Glories Alexandra, Amalric François, Girard Jean-Philippe
机构信息
Laboratoire de Biologie Vasculaire, Institut de Pharmacologie et de Biologie Structurale, CNRS UMR 5089, 205 route de Narbonne, 31077 Toulouse, France.
出版信息
Trends Biochem Sci. 2003 Feb;28(2):66-9. doi: 10.1016/S0968-0004(02)00013-0.
We have identified a novel evolutionarily conserved protein motif - designated the THAP domain - that defines a new family of cellular factors. We have found that the THAP domain presents striking similarities with the site-specific DNA-binding domain (DBD) of Drosophila P element transposase, including a similar size, N-terminal location, and conservation of the residues that define the THAP motif, such as the C2CH signature (Cys-Xaa(2-4)-Cys-Xaa(35-50)-Cys-Xaa(2)-His). Our results suggest that the THAP domain is a novel example of a DBD that is shared between cellular proteins and transposases from mobile genomic parasites.
我们鉴定出一种新的进化上保守的蛋白质基序——命名为THAP结构域——它定义了一个新的细胞因子家族。我们发现，THAP结构域与果蝇P因子转座酶的位点特异性DNA结合结构域（DBD）具有显著相似性，包括相似的大小、N端位置以及定义THAP基序的残基的保守性，如C2CH特征序列（半胱氨酸-任意氨基酸（2-4个）-半胱氨酸-任意氨基酸（35-50个）-半胱氨酸-任意氨基酸（2个）-组氨酸）。我们的结果表明，THAP结构域是一种新型的DBD，它存在于细胞蛋白和来自移动基因组寄生虫的转座酶之间。
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