Ubiquitin-specific peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity.
Ubiquitin-specific peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity.
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泛素特异性肽酶42（USP42）的功能可供脱征组蛋白并调节转录活性。
DOI：
10.1074/jbc.m114.589267
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发表时间：
2014-12-12
期刊：
影响因子：
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通讯作者：
Vousden KH
中科院分区：
文献类型：
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作者：
Hock AK;Vigneron AM;Vousden KH
背景：组蛋白的泛素修饰调节基因表达。结果：USP42靶向组蛋白H2B启动子，导致泛素化降低。这与由许多转录因子驱动的转录调节相关。结论：USP42参与了转录调控。意义：组蛋白H2B作为USP 42靶点的鉴定扩展了我们对调控基因表达的因子的理解。泛素特异性肽酶42（USP 42）是一种去泛素化酶，可以靶向p53并有助于p53在应激反应中的稳定。我们现在发现USP42也可以独立于p53调节转录。USP42与RNA聚合酶II（RNA Pol II）共定位于核灶中，与组蛋白H2B和去泛素化H2B结合。USP42的缺失增加了模型启动子处的H2B泛素化，并降低了许多启动子的基础和诱导转录。这些结果与USP 42通过去泛素化组蛋白调节转录的作用一致。
Background: Ubiquitin modification of histones regulates gene expression. Results: USP42 targets histone H2B at promoters, leading to decreased ubiquitylation. This correlates with the regulation of transcription driven by a number of transcription factors. Conclusion: USP42 contributes to the modulation of transcription. Significance: The identification of histone H2B as a target for USP42 extends our understanding of the factors that can regulate gene expression. Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear foci, bound to histone H2B, and deubiquitylated H2B. Depletion of USP42 increased H2B ubiquitylation at a model promoter and decreased both basal and induced transcription from a number of promoters. These results are consistent with a role for USP42 in regulating transcription by deubiquitylating histones.