免疫球蛋白重链增强子处碱性螺旋-环-螺旋-亮氨酸拉链蛋白的选择性利用
Selective utilization of basic helix-loop-helix-leucine zipper proteins at the immunoglobulin heavy-chain enhancer.
作者信息
Carter R S, Ordentlich P, Kadesch T
机构信息
Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6145, USA.
出版信息
Mol Cell Biol. 1997 Jan;17(1):18-23. doi: 10.1128/MCB.17.1.18.
Abstract
The microE3 E box within the immunoglobulin heavy-chain (IgH) enhancer binds several proteins of the basic helix-loop-helix-leucine zipper (bHLHzip) class, including TFE3, USF1, and Max. Both TFE3 and USF have been described as transcriptional activators, and so we investigated their possible roles in activating the IgH enhancer in vivo. Although TFE3 activated various enhancer-based reporters, both USF1 and Max effectively inhibited transcription. Inhibition by USF correlated with the lack of a strong activation domain and was the result of the protein neutralizing the microE3 site. The effects of dominant-negative derivatives of TFE3 and USF1 confirmed that TFE3, or a TFE3-like protein, is the primary cellular bHLHzip protein that activates the IgH enhancer. In addition to providing a physiological role for TFE3, our results call into question the traditional view of USF1 as an obligate transcriptional activator.
摘要
免疫球蛋白重链（IgH）增强子内的微小E3 E盒结合了几种属于碱性螺旋-环-螺旋-亮氨酸拉链（bHLHzip）类的蛋白质，包括TFE3、USF1和Max。TFE3和USF都被描述为转录激活因子，因此我们研究了它们在体内激活IgH增强子的可能作用。尽管TFE3激活了各种基于增强子的报告基因，但USF1和Max都有效地抑制了转录。USF的抑制作用与缺乏强激活结构域有关，是该蛋白中和微小E3位点的结果。TFE3和USF1的显性负性衍生物的作用证实，TFE3或类似TFE3的蛋白是激活IgH增强子的主要细胞bHLHzip蛋白。除了为TFE3提供生理作用外，我们的结果还对USF1作为专一性转录激活因子的传统观点提出了质疑。
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