REDOX REGULATION OF FOS AND JUN DNA-BINDING ACTIVITY INVITRO
REDOX REGULATION OF FOS AND JUN DNA-BINDING ACTIVITY INVITRO
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DOI：
10.1126/science.2118682
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发表时间：
1990-09-07
期刊：
影响因子：
56.9
通讯作者：
CURRAN, T
中科院分区：
文献类型：
--
作者：
ABATE, C;PATEL, L;CURRAN, T
原癌基因 c-fos 和 c-jun 在信号转导过程中协同发挥诱导转录因子的作用。他们的蛋白质产物 Fos 和 Jun 形成异二聚体复合物，与称为激活蛋白 1 (AP-1) 结合位点的 DNA 调控元件发生相互作用。二聚化通过亮氨酸拉链结构域之间的相互作用发生，并用于使每个蛋白质中富含碱性氨基酸的区域正确并置，并形成 DNA 结合结构域。 Fos-Jun 异二聚体的 DNA 结合通过两种蛋白质 DNA 结合域中单个保守半胱氨酸残基的还原-氧化 (redox) 来调节。此外，还鉴定出一种核蛋白可以减少 Fos 和 Jun 并刺激体外 DNA 结合活性。这些结果表明 AP-1 结合因子介导的转录活性可能受到氧化还原机制的调节。
The proto-oncogenes c-fos and c-jun function cooperatively as inducible transcription factors in signal transduction processes. Their protein products, Fos and Jun, form a heterodimeric complex that ineracts with the DNA regulatory element known as the activator protein-1 (AP-1) binding site. Dimerization occurs via interaction between leucine zipper domains and serves to bring into proper juxtaposition a region in each protein that is rich in basic amino acids and that forms a DNA-binding domain. DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation (redox) of a single conserved cysteine residue in the DNA-binding domains of the two proteins. Furthermore, a nuclear protein was identified that reduced Fos and Jun and stimulated DNA-binding activity in vitro. These results suggest that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism.