转录因子共激活因子C1（HCF）的自催化蛋白水解：共激活因子功能蛋白水解调节的潜在作用
Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function.
作者信息
Vogel J L, Kristie T M
机构信息
Laboratory of Viral Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
出版信息
Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9425-30. doi: 10.1073/pnas.160266697.
Abstract
Site-specific proteolysis is an important biological mechanism for the regulation of cellular processes such as gene expression, cell signaling, development, and apoptosis. In transcriptional regulation, specific proteolysis regulates the localization and activity of many regulatory factors. The C1 factor (HCF), a cellular transcription factor and coactivator, undergoes site-specific proteolytic processing at a series of unusual amino acid reiterations to generate a family of amino- and carboxyl-terminal polypeptides that remain tightly associated. Expression and purification of bacterially expressed domains of the C1 factor identifies an autocatalytic activity that is responsible for the specific cleavage of the reiterations. In addition, coexpression of the autocatalytic domain with a heterologous protein containing a target cleavage site demonstrates that the C1 protease may also function in trans.
摘要
位点特异性蛋白水解是调节细胞过程（如基因表达、细胞信号传导、发育和细胞凋亡）的重要生物学机制。在转录调控中，特异性蛋白水解调节许多调节因子的定位和活性。C1因子（HCF）是一种细胞转录因子和共激活因子，在一系列不寻常的氨基酸重复序列处进行位点特异性蛋白水解加工，以产生紧密相关的氨基末端和羧基末端多肽家族。C1因子细菌表达结构域的表达和纯化鉴定出一种自催化活性，该活性负责重复序列的特异性切割。此外，自催化结构域与含有靶切割位点的异源蛋白的共表达表明，C1蛋白酶也可能在反式作用中发挥作用。
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