摘要
组蛋白构成蛋白质最古老的家族之一,并且在真核生物进化中非常保守,这一点早在一个世纪前就被发现。然而,仅近30年才证明了组蛋白的影响力远超于包装DNA。为创建高等真核生物DNA功能所需的多种染色体结构,组蛋白进行翻译后修饰。许多这种修饰被完好记录,而其他的,如组蛋白尾部裂解,则很少被熟知。近期研究已发现了一些裂解组蛋白的蛋白酶,暗示了其在除感染和炎症外的干细胞分化和衰老中剪除组蛋白的作用,然而潜在机制还不清楚。一类组蛋白,尤其是组蛋白H3,由于它的大量N-末端修饰点和自我平衡调节进程的普遍而受关注。带着对H3的特殊考虑,我们在这里将讨论关于组蛋白蛋白裂解的新发现和其在免疫学和表观遗传学研究中的意义。
关键词: 裂解,组蛋白,H3,翻译后修饰
Current Molecular Medicine
Title:Histone Cleavage as a Mechanism for Epigenetic Regulation: Current Insights and Perspectives
Volume: 14 Issue: 9
Author(s): P. Zhou, E. Wu, H.B. Alam and Y. Li
Affiliation:
关键词: 裂解,组蛋白,H3,翻译后修饰
摘要: Discovered over a century ago, histones constitute one of the oldest families of proteins and have been remarkably conserved throughout eukaryotic evolution. However, only for the past 30 years have histones demonstrated that their influence extends far beyond packaging DNA. To create the various chromatin structures that are necessary for DNA function in higher eukaryotes, histones undergo posttranslational modifications. While many such modifications are well documented, others, such as histone tail cleavage are less understood. Recent studies have discovered several proteases that cleave histones and have suggested roles for clipped histones in stem cell differentiation and aging in addition to infection and inflammation; the underlying mechanisms, however, are uncertain. One histone class in particular, histone H3, has received outstanding interest due to its numerous N-terminal modification sites and prevalence in regulating homeostatic processes. Here, with special consideration of H3, we will discuss the novel findings regarding histone proteolytic cleavage as well as their significance in the studies of immunology and epigenetics.
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Cite this article as:
Zhou P., Wu E., Alam H.B. and Li Y., Histone Cleavage as a Mechanism for Epigenetic Regulation: Current Insights and Perspectives, Current Molecular Medicine 2014; 14 (9) . https://dx.doi.org/10.2174/1566524014666141015155630
DOI https://dx.doi.org/10.2174/1566524014666141015155630 |
Print ISSN 1566-5240 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5666 |
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