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Study of the N-Terminal Domain Homodimerization in Human Proteins with Zinc Finger Clusters
Doklady Biochemistry and Biophysics ( IF 0.8 ) Pub Date : 2021-08-23 , DOI: 10.1134/s1607672921040050
D V Fursenko 1 , P G Georgiev 1 , A N Bonchuk 1
Affiliation  

Abstract

CTCF belongs to a large family of transcription factors with clusters of C2H2-type zinc finger domains (C2H2 proteins) and is a main architectural protein in mammals. Human CTCF has a homodimerizing unstructured domain at the N-terminus which is involved in long-distance interactions. To test the presence of similar N-terminal domains in other human C2H2 proteins, a yeast two-hybrid system was used. In total, the ability of unstructured N-terminal domains to homodimerize was investigated for six human C2H2 proteins with an expression profile similar to CTCF. The data indicate the lack of the homodimerization ability of these domains. On the other hand, three C2H2 proteins containing the structured domain DUF3669 at the N-terminus demonstrated homo- and heterodimerization activity.



中文翻译:


人类蛋白质锌指簇 N 端结构域同二聚化的研究


 抽象的


CTCF属于具有C2H2型锌指结构域簇(C2H2蛋白)的转录因子大家族,是哺乳动物中的主要结构蛋白。人类 CTCF 在 N 末端有一个同二聚化非结构化结构域,参与长距离相互作用。为了测试其他人类 C2H2 蛋白中是否存在类似的 N 端结构域,使用了酵母双杂交系统。总的来说,针对表达谱与 CTCF 相似的六种人 C2H2 蛋白,研究了非结构化 N 端结构域同二聚化的能力。数据表明这些结构域缺乏同二聚化能力。另一方面,N 末端含有结构域 DUF3669 的三种 C2H2 蛋白表现出同源二聚化和异源二聚化活性。

更新日期:2021-08-24
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