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信号转导和转录激活因子氨基末端结构域赋予的协同DNA结合和序列选择性识别

Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain.

作者信息

Xu X, Sun Y L, Hoey T

机构信息

Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.

出版信息

Science. 1996 Aug 9;273(5276):794-7. doi: 10.1126/science.273.5276.794.

DOI:10.1126/science.273.5276.794
PMID:8670419
Abstract

STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of STAT proteins was required for cooperative DNA binding, although this domain was not essential for dimerization or binding to a single site. Cooperative binding interactions enabled the STAT proteins to recognize variations of the consensus site. These sites can be specific for the different STAT proteins and may function to direct selective transcriptional activation.

摘要

信号转导与转录激活因子(STAT)蛋白尽管具有相似的DNA结合偏好,但仍能激活不同的靶基因。我们在干扰素-γ基因附近的天然STAT结合位点上研究了STAT蛋白的转录特异性。这些位点以多个拷贝排列,并且STAT结合需要协同相互作用。STAT蛋白保守的氨基末端结构域是协同DNA结合所必需的,尽管该结构域对于二聚化或与单个位点的结合并非必不可少。协同结合相互作用使STAT蛋白能够识别共有位点的变体。这些位点可能对不同的STAT蛋白具有特异性,并可能起到指导选择性转录激活的作用。

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