Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States of America.
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States of America.
Biochim Biophys Acta Gene Regul Mech. 2024 Jun;1867(2):195018. doi: 10.1016/j.bbagrm.2024.195018. Epub 2024 Feb 6.
Nucleosomes are major determinants of eukaryotic genome organization and regulation. Many studies, incorporating a diversity of experimental approaches, have been focused on identifying and discerning the contributions of histone post-translational modifications to DNA-centered processes. Among these, monoubiquitylation of H2B (H2Bub) on K120 in humans or K123 in budding yeast is a critical histone modification that has been implicated in a wide array of DNA transactions. H2B is co-transcriptionally ubiquitylated and deubiquitylated via the concerted action of an extensive network of proteins. In addition to altering the chemical and physical properties of the nucleosome, H2Bub is important for the proper control of gene expression and for the deposition of other histone modifications. In this review, we discuss the molecular mechanisms underlying the ubiquitylation cycle of H2B and how it connects to the regulation of transcription and chromatin structure.
核小体是真核生物基因组组织和调控的主要决定因素。许多研究采用了多种实验方法,致力于识别和辨别组蛋白翻译后修饰对以 DNA 为中心的过程的贡献。其中,人类 H2B 上 K120 或芽殖酵母上 K123 的单泛素化(H2Bub)是一种关键的组蛋白修饰,它与广泛的 DNA 交易有关。H2B 通过广泛的蛋白质网络的协同作用被转录共泛素化和去泛素化。除了改变核小体的化学和物理性质外,H2Bub 对于基因表达的正确控制和其他组蛋白修饰的沉积也很重要。在这篇综述中,我们讨论了 H2B 泛素化循环的分子机制,以及它如何与转录和染色质结构的调控联系起来。