Holt Matthew V, Wang Tao, Young Nicolas L
Verna & Marrs McLean Department of Biochemistry & Molecular Biology, Baylor College of Medicine, Houston, Texas.
Current Address: Clinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, Washington.
Curr Protoc. 2021 Feb;1(2):e26. doi: 10.1002/cpz1.26.
Histones are the primary protein component of chromatin and are involved in virtually all DNA-templated processes. Histones are abundantly post-translationally modified by a variety of chromatin-modifying machinery. These post-translational modifications (PTMs) are recognized by a range of "reader" proteins, which recruit additional proteins to specific locations on chromatin and impart precise and powerful effects on gene regulation. Each PTM typically exerts a positive or negative effect on transcription, and recent studies have shown that histone PTMs function in a combinatorial histone code: that is, histone PTMs function in combination to exert precise DNA-templated regulation. Thus, there is a need to identify and understand proteoforms, or unambiguously defined single protein molecules with all combinations of modifications. Top-down proteomics is currently the only viable approach for identifying and quantitating histone proteoforms, and mass spectrometry instruments have become sufficiently powerful to perform these quantitative analyses in a robust and high-throughput fashion. These recent innovations have enabled new experimental directions in chromatin research but have also introduced temporal and other constraints. This has led us to develop the protocols described here, which increase throughput, reduce sample requirements, and maintain robust quantitation. Although originally designed for high-throughput quantitative top-down proteomics, the protocols described here are useful for a wide range of chromatin biology applications. Starting with small amounts of cells or tissue, we describe two basic protocols for exceptionally rapid and efficient nuclei isolation, acid extraction of histones, and high-performance liquid chromatography fractionation of histones into histone families. We additionally describe the quantitative top-down proteomic analysis of histone H4 proteoforms. © 2021 Wiley Periodicals LLC. Basic Protocol 1: Nuclei isolation and acid extraction of histones from mammalian cells in culture/tissues Basic Protocol 2: HPLC fractionation of histones and histone H4 HPLC-MS/MS Support Protocol: Preparation of intact H3 histone tails by Glu-C digestion.
组蛋白是染色质的主要蛋白质成分,几乎参与所有以DNA为模板的过程。组蛋白在翻译后会被多种染色质修饰机制大量修饰。这些翻译后修饰(PTMs)被一系列“读取器”蛋白识别,这些蛋白将其他蛋白招募到染色质上的特定位置,并对基因调控产生精确而强大的影响。每种PTM通常对转录产生正向或负向影响,最近的研究表明,组蛋白PTMs以组合组蛋白密码的形式发挥作用:也就是说,组蛋白PTMs共同发挥作用以实现精确的以DNA为模板的调控。因此,有必要识别和理解蛋白质异构体,即具有所有修饰组合的明确界定的单个蛋白质分子。自上而下的蛋白质组学是目前识别和定量组蛋白蛋白质异构体的唯一可行方法,质谱仪器已经足够强大,能够以稳健且高通量的方式进行这些定量分析。这些最新的创新为染色质研究带来了新的实验方向,但也引入了时间和其他限制。这促使我们开发了此处所述的方案,该方案提高了通量,减少了样品需求,并保持了稳健的定量。尽管此处所述的方案最初是为高通量定量自上而下蛋白质组学设计的,但对于广泛的染色质生物学应用也很有用。从小量细胞或组织开始,我们描述了两种基本方案,用于极其快速和高效地分离细胞核、酸提取组蛋白,以及通过高效液相色谱将组蛋白分离成组蛋白家族。我们还描述了组蛋白H4蛋白质异构体的定量自上而下蛋白质组学分析。©2021威利期刊公司。基本方案1:从培养的哺乳动物细胞/组织中分离细胞核并酸提取组蛋白 基本方案2:组蛋白和组蛋白H4的高效液相色谱分离 高效液相色谱-串联质谱 支持方案:通过Glu-C消化制备完整的H3组蛋白尾巴