The micronuclear histone H3 clipping in the unicellular eukaryote Tetrahymena thermophila.

IF 5.8 2区 生物学 Q1 MARINE & FRESHWATER BIOLOGY
Marine Life Science & Technology Pub Date : 2022-11-24 eCollection Date: 2022-11-01 DOI:10.1007/s42995-022-00151-0
Fan Wei, Bo Pan, Jinghan Diao, Yuanyuan Wang, Yalan Sheng, Shan Gao
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引用次数: 0

Abstract

Clipping of the histone H3 N-terminal tail has been implicated in multiple fundamental biological processes for a growing list of eukaryotes. H3 clipping, serving as an irreversible process to permanently remove some post-translational modifications (PTMs), may lead to noticeable changes in chromatin dynamics or gene expression. The eukaryotic model organism Tetrahymena thermophila is among the first few eukaryotes that exhibits H3 clipping activity, wherein the first six amino acids of H3 are cleaved off during vegetative growth. Clipping only occurs in the transcriptionally silent micronucleus of the binucleated T. thermophila, thus offering a unique opportunity to reveal the role of H3 clipping in epigenetic regulation. However, the physiological functions of the truncated H3 and its protease(s) for clipping remain elusive. Here, we review the major findings of H3 clipping in T. thermophila and highlight its association with histone modifications and cell cycle regulation. We also summarize the functions and mechanisms of H3 clipping in other eukaryotes, focusing on the high diversity in terms of protease families and cleavage sites. Finally, we predict several protease candidates in T. thermophila and provide insights for future studies.

Supplementary information: The online version contains supplementary material available at 10.1007/s42995-022-00151-0.

单细胞真核生物嗜热四膜虫的微核组蛋白H3剪切。
组蛋白H3 n端尾部的剪切与越来越多的真核生物的多个基本生物过程有关。H3剪切作为永久去除一些翻译后修饰(ptm)的不可逆过程,可能导致染色质动力学或基因表达的显著变化。真核模式生物嗜热四膜虫是最早表现出H3剪切活性的真核生物之一,其中H3的前六个氨基酸在营养生长过程中被剪切掉。剪接仅发生在双核嗜热t细胞转录沉默的微核中,从而为揭示H3剪接在表观遗传调控中的作用提供了独特的机会。然而,截断的H3及其蛋白酶的剪切生理功能仍然难以捉摸。在这里,我们回顾了嗜热t细胞中H3剪切的主要发现,并强调了它与组蛋白修饰和细胞周期调节的关系。我们还总结了其他真核生物中H3剪切的功能和机制,重点介绍了蛋白酶家族和切割位点的高度多样性。最后,我们预测了嗜热t的几种候选蛋白酶,并为未来的研究提供了见解。补充信息:在线版本包含补充资料,下载地址为10.1007/s42995-022-00151-0。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Marine Life Science & Technology
Marine Life Science & Technology MARINE & FRESHWATER BIOLOGY-
CiteScore
9.60
自引率
10.50%
发文量
58
期刊介绍: Marine Life Science & Technology (MLST), established in 2019, is dedicated to publishing original research papers that unveil new discoveries and theories spanning a wide spectrum of life sciences and technologies. This includes fundamental biology, fisheries science and technology, medicinal bioresources, food science, biotechnology, ecology, and environmental biology, with a particular focus on marine habitats. The journal is committed to nurturing synergistic interactions among these diverse disciplines, striving to advance multidisciplinary approaches within the scientific field. It caters to a readership comprising biological scientists, aquaculture researchers, marine technologists, biological oceanographers, and ecologists.
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