{"title":"由高度差异组蛋白构建的核小体结构:寄生虫和巨型 DNA 病毒。","authors":"Shoko Sato, Mariko Dacher, Hitoshi Kurumizaka","doi":"10.3390/epigenomes6030022","DOIUrl":null,"url":null,"abstract":"<p><p>In eukaryotes, genomic DNA is bound with histone proteins and packaged into chromatin. The nucleosome, a fundamental unit of chromatin, regulates the accessibility of DNA to enzymes involved in gene regulation. During the past few years, structural analyses of chromatin architectures have been limited to evolutionarily related organisms. The amino acid sequences of histone proteins are highly conserved from humans to yeasts, but are divergent in the deeply branching protozoan groups, including human parasites that are directly related to human health. Certain large DNA viruses, as well as archaeal organisms, contain distant homologs of eukaryotic histone proteins. The divergent sequences give rise to unique and distinct nucleosome architectures, although the fundamental principles of histone folding and DNA contact are highly conserved. In this article, we review the structures and biophysical properties of nucleosomes containing histones from the human parasites <i>Giardia lamblia</i> and <i>Leishmania major</i>, and histone-like proteins from the <i>Marseilleviridae</i> amoeba virus family. The presented data confirm the sharing of the overall DNA compaction system among evolutionally distant species and clarify the deviations from the species-specific nature of the nucleosome.</p>","PeriodicalId":55768,"journal":{"name":"Epigenomes","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2022-08-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9396995/pdf/","citationCount":"0","resultStr":"{\"title\":\"Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses.\",\"authors\":\"Shoko Sato, Mariko Dacher, Hitoshi Kurumizaka\",\"doi\":\"10.3390/epigenomes6030022\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>In eukaryotes, genomic DNA is bound with histone proteins and packaged into chromatin. The nucleosome, a fundamental unit of chromatin, regulates the accessibility of DNA to enzymes involved in gene regulation. During the past few years, structural analyses of chromatin architectures have been limited to evolutionarily related organisms. The amino acid sequences of histone proteins are highly conserved from humans to yeasts, but are divergent in the deeply branching protozoan groups, including human parasites that are directly related to human health. Certain large DNA viruses, as well as archaeal organisms, contain distant homologs of eukaryotic histone proteins. The divergent sequences give rise to unique and distinct nucleosome architectures, although the fundamental principles of histone folding and DNA contact are highly conserved. In this article, we review the structures and biophysical properties of nucleosomes containing histones from the human parasites <i>Giardia lamblia</i> and <i>Leishmania major</i>, and histone-like proteins from the <i>Marseilleviridae</i> amoeba virus family. The presented data confirm the sharing of the overall DNA compaction system among evolutionally distant species and clarify the deviations from the species-specific nature of the nucleosome.</p>\",\"PeriodicalId\":55768,\"journal\":{\"name\":\"Epigenomes\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.5000,\"publicationDate\":\"2022-08-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9396995/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Epigenomes\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3390/epigenomes6030022\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"GENETICS & HEREDITY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Epigenomes","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/epigenomes6030022","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"GENETICS & HEREDITY","Score":null,"Total":0}
引用次数: 0
摘要
在真核生物中,基因组 DNA 与组蛋白结合并包装成染色质。核小体是染色质的基本单位,它调节 DNA 对参与基因调控的酶的可及性。在过去几年中,染色质结构分析仅限于与生物进化相关的生物。从人类到酵母,组蛋白的氨基酸序列高度保守,但在分支繁多的原生动物群(包括与人类健康直接相关的人类寄生虫)中却存在差异。某些大型 DNA 病毒和古生物含有与真核组蛋白遥远的同源物。尽管组蛋白折叠和 DNA 接触的基本原理高度保守,但不同的序列产生了独特的核小体结构。在这篇文章中,我们回顾了含有人类寄生虫蓝氏贾第鞭毛虫和大利什曼原虫组蛋白的核小体以及马赛病毒科变形虫病毒家族的组蛋白样蛋白的结构和生物物理特性。所提供的数据证实了进化遥远的物种之间共享整体 DNA 压实系统,并澄清了核小体的物种特异性偏差。
Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses.
In eukaryotes, genomic DNA is bound with histone proteins and packaged into chromatin. The nucleosome, a fundamental unit of chromatin, regulates the accessibility of DNA to enzymes involved in gene regulation. During the past few years, structural analyses of chromatin architectures have been limited to evolutionarily related organisms. The amino acid sequences of histone proteins are highly conserved from humans to yeasts, but are divergent in the deeply branching protozoan groups, including human parasites that are directly related to human health. Certain large DNA viruses, as well as archaeal organisms, contain distant homologs of eukaryotic histone proteins. The divergent sequences give rise to unique and distinct nucleosome architectures, although the fundamental principles of histone folding and DNA contact are highly conserved. In this article, we review the structures and biophysical properties of nucleosomes containing histones from the human parasites Giardia lamblia and Leishmania major, and histone-like proteins from the Marseilleviridae amoeba virus family. The presented data confirm the sharing of the overall DNA compaction system among evolutionally distant species and clarify the deviations from the species-specific nature of the nucleosome.