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预测的分子结构表明,CTF/NF-I可能作为组蛋白乙酰转移酶发挥作用。

The predicted molecular structure suggests that CTF/NF-I may function as a histone acetylase.

作者信息

Oikarinen J, Mannermaa R M

机构信息

Collagen Research Unit, Biocenter, Oulu, Finland.

出版信息

FEBS Lett. 1990 Oct 29;273(1-2):11-4. doi: 10.1016/0014-5793(90)81039-q.

Abstract

The primary structure of nuclear factor-I (CTF/NF-I), a eukaryotic regulatory DNA-binding protein involved in both DNA replication and gene transcription, and the secondary structure predictable from it, are compared here with those of a number of prokaryotic acetylases. Hydropathy and Chou-Fasman analyses reveal that the polypeptide chain of CTF/NF-I is likely to fold to higher order structures similar to those of the acetylases, and significant conservation of functionally important regions of the acetylases is observed in CTF/NF-I. It is therefore suggested that CTF/NF-I may function as a histone acetylase.

摘要

核因子-I(CTF/NF-I)是一种参与DNA复制和基因转录的真核调节性DNA结合蛋白,本文将其一级结构以及由此预测的二级结构与多种原核乙酰化酶的结构进行了比较。亲水性和Chou-Fasman分析表明,CTF/NF-I的多肽链可能折叠成与乙酰化酶类似的高级结构,并且在CTF/NF-I中观察到了乙酰化酶功能重要区域的显著保守性。因此,有人提出CTF/NF-I可能作为组蛋白乙酰化酶发挥作用。

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