{"title":"酵母 COMPASS 和人类混系白血病 (MLL) 的核心复合物，核小体的结构、功能和识别。","authors":"Uhn-Soo Cho","doi":"10.1007/978-3-031-58843-3_6","DOIUrl":null,"url":null,"abstract":"<p><p>Yeast COMPASS (complex of proteins associated with Set1) and human MLL (mixed-lineage leukemia) complexes are histone H3 lysine 4 methyltransferases with critical roles in gene regulation and embryonic development. Both complexes share a conserved C-terminal SET domain, responsible for catalyzing histone H3 K4 methylation on nucleosomes. Notably, their catalytic activity toward nucleosomes is enhanced and optimized with assembly of auxiliary subunits. In this review, we aim to illustrate the recent X-ray and cryo-EM structures of yeast COMPASS and human MLL1 core complexes bound to either unmodified nucleosome core particle (NCP) or H2B mono-ubiquitinated NCP (H2Bub.NCP). We further delineate how each auxiliary component of the complex contributes to the NCP and ubiquitin recognition to maximize the methyltransferase activity.</p>","PeriodicalId":21991,"journal":{"name":"Sub-cellular biochemistry","volume":"104 ","pages":"101-117"},"PeriodicalIF":0.0000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The Core Complex of Yeast COMPASS and Human Mixed-Lineage Leukemia (MLL), Structure, Function, and Recognition of the Nucleosome.\",\"authors\":\"Uhn-Soo Cho\",\"doi\":\"10.1007/978-3-031-58843-3_6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Yeast COMPASS (complex of proteins associated with Set1) and human MLL (mixed-lineage leukemia) complexes are histone H3 lysine 4 methyltransferases with critical roles in gene regulation and embryonic development. Both complexes share a conserved C-terminal SET domain, responsible for catalyzing histone H3 K4 methylation on nucleosomes. Notably, their catalytic activity toward nucleosomes is enhanced and optimized with assembly of auxiliary subunits. In this review, we aim to illustrate the recent X-ray and cryo-EM structures of yeast COMPASS and human MLL1 core complexes bound to either unmodified nucleosome core particle (NCP) or H2B mono-ubiquitinated NCP (H2Bub.NCP). We further delineate how each auxiliary component of the complex contributes to the NCP and ubiquitin recognition to maximize the methyltransferase activity.</p>\",\"PeriodicalId\":21991,\"journal\":{\"name\":\"Sub-cellular biochemistry\",\"volume\":\"104 \",\"pages\":\"101-117\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Sub-cellular biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/978-3-031-58843-3_6\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Sub-cellular biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/978-3-031-58843-3_6","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
摘要
酵母 COMPASS（与 Set1 相关的蛋白复合物）和人类 MLL（混合系白血病）复合物是组蛋白 H3 赖氨酸 4 甲基转移酶，在基因调控和胚胎发育中起着关键作用。这两种复合物都有一个保守的 C 端 SET 结构域，负责催化核小体上的组蛋白 H3 K4 甲基化。值得注意的是，通过组装辅助亚基，它们对核小体的催化活性得到了增强和优化。在这篇综述中，我们旨在说明酵母 COMPASS 和人类 MLL1 核心复合物与未修饰的核小体核心颗粒（NCP）或 H2B 单泛素化 NCP（H2Bub.NCP）结合的最新 X 射线和低温电子显微镜结构。我们进一步阐明了复合物中的每个辅助成分如何促进 NCP 和泛素识别，以最大限度地提高甲基转移酶的活性。
The Core Complex of Yeast COMPASS and Human Mixed-Lineage Leukemia (MLL), Structure, Function, and Recognition of the Nucleosome.
Yeast COMPASS (complex of proteins associated with Set1) and human MLL (mixed-lineage leukemia) complexes are histone H3 lysine 4 methyltransferases with critical roles in gene regulation and embryonic development. Both complexes share a conserved C-terminal SET domain, responsible for catalyzing histone H3 K4 methylation on nucleosomes. Notably, their catalytic activity toward nucleosomes is enhanced and optimized with assembly of auxiliary subunits. In this review, we aim to illustrate the recent X-ray and cryo-EM structures of yeast COMPASS and human MLL1 core complexes bound to either unmodified nucleosome core particle (NCP) or H2B mono-ubiquitinated NCP (H2Bub.NCP). We further delineate how each auxiliary component of the complex contributes to the NCP and ubiquitin recognition to maximize the methyltransferase activity.
期刊介绍：
The book series SUBCELLULAR BIOCHEMISTRY is a renowned and well recognized forum for disseminating advances of emerging topics in Cell Biology and related subjects. All volumes are edited by established scientists and the individual chapters are written by experts on the relevant topic. The individual chapters of each volume are fully citable and indexed in Medline/Pubmed to ensure maximum visibility of the work.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
