Mammalian DNA cytosine‐5 methyltransferase interacts with p23 protein

FEBS Letters

Verdine, Gregory L.²  Zhang, Xiaoyan¹ 

[1] Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA;Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA

关键词: Mammalian DNA cytosine-5 methyltransferase;    p23 protein;    Yeast two-hybrid system;    Protein-protein interaction;    MTase;    mammalian DNA cytosine-5 methyltransferase;    GST;    glutathione S-transferase;    X-Gal;    5-bromo-4-chloro-2indolyl β-d-galactoside;    MEL;    murine erythroleukemia cell;    PR;    progesterone receptor;   

DOI  :  10.1016/0014-5793(96)00810-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In higher eukaryotic genomes, methylated cytosine residues (m⁵C) are distributed in heritable, cell-type-specific patterns, which are believed to be involved in the control of gene expression, developmental regulation and genomic imprinting. These methylation patterns are established and maintained by DNA cytosine-5 methyltransferase (MTase), a ∼1500 amino acid enzyme containing a regulatory N-terminal domain and a catalytic C-terminal domain. The mechanism responsible for targeting MTase to particular genes is poorly understood and might possibly involve interactions with other proteins. In an effort to identify proteins that interact with the mammalian MTase, we used the yeast two-hybrid system with several different MTase domains as baits. Here we report an interaction between the C-terminal catalytic domain of the MTase and p23, a protein previously reported to associate with the progesterone receptor (PR) complex.

【 授权许可】

Unknown