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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors
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Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors

机译：转录共激活因子HCF-1的位点特异性蛋白水解可以调节其与蛋白质辅因子的相互作用

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摘要

Limited proteolytic processing is an important transcriptional regulatory mechanism. In various contexts, proteolysis controls the cytoplasmic-to-nuclear transport of important transcription factors or removes domains to produce factors with altered activities. The transcriptional coactivator host cell factor-1 (HCF-1) is proteolytically processed within a unique domain consisting of 20-aa reiterations. Site-specific cleavage within one or more repeats generates a family of amino- and carboxyl-terminal subunits that remain tightly associated. However, the consequences of HCF-1 processing have been undefined. In this study, it was determined that the HCF-1-processing domain interacts with several proteins including the transcriptional coactivator/corepressor four-and-a-half LIM domain-2 (FHL2). Analysis of this interaction has uncovered specificity with both sequence and context determinants within the reiterations of this processing domain. In cells, FHL2 interacts exclusively with the nonprocessed coactivator and costimulates transcription of an HCF-1-dependent target gene. The functional interaction of HCF-1 with FHL2 supports a model in which site-specific proteolysis regulates the interaction of HCF-1 with protein partners and thus can modulate the activity of this coactivator. This paradigm expands the biological significance of limited proteolytic processing as a regulatory mechanism in gene transcription.
机译：有限的蛋白水解加工是重要的转录调节机制。在各种情况下，蛋白水解控制重要转录因子从细胞质到核的运输，或去除结构域以产生活性改变的因子。转录共激活因子宿主细胞因子1（HCF-1）在由20个氨基酸重复组成的唯一域中进行蛋白水解处理。一个或多个重复序列中的位点特异性裂解产生了一个氨基和羧基末端亚基家族，它们仍然紧密相连。但是，HCF-1处理的后果尚未确定。在这项研究中，已确定HCF-1加工域与几种蛋白相互作用，包括转录共激活因子/共抑制因子四半LIM域2（FHL2）。在此处理域的重复中，对这种相互作用的分析发现了序列和上下文决定因素的特异性。在细胞中，FHL2仅与未加工的共激活因子相互作用，并共同刺激HCF-1依赖性靶基因的转录。 HCF-1与FHL2的功能相互作用支持一种模型，其中位点特异性蛋白水解调节HCF-1与蛋白质伴侣的相互作用，因此可以调节该共激活因子的活性。这种范例扩展了有限的蛋白水解过程作为基因转录调控机制的生物学意义。

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