What is the role of histone H1 heterogeneity? A functional model emerges from a 50 year mystery.

IF 1.1 Q4 BIOPHYSICS
AIMS Biophysics Pub Date : 2015-01-01 Epub Date: 2015-11-16 DOI:10.3934/biophy.2015.4.724
Missag Hagop Parseghian
{"title":"What is the role of histone H1 heterogeneity? A functional model emerges from a 50 year mystery.","authors":"Missag Hagop Parseghian","doi":"10.3934/biophy.2015.4.724","DOIUrl":null,"url":null,"abstract":"<p><p>For the past 50 years, understanding the function of histone H1 heterogeneity has been mired in confusion and contradiction. Part of the reason for this is the lack of a working model that tries to explain the large body of data that has been collected about the H1 subtypes so far. In this review, a global model is described largely based on published data from the author and other researchers over the past 20 years. The intrinsic disorder built into H1 protein structure is discussed to help the reader understand that these histones are multi-conformational and adaptable to interactions with different targets. We discuss the role of each structural section of H1 (as we currently understand it), but we focus on the H1's C-terminal domain and its effect on each subtype's affinity, mobility and compaction of chromatin. We review the multiple ways these characteristics have been measured from circular dichroism to FRAP analysis, which has added to the sometimes contradictory assumptions made about each subtype. Based on a tabulation of these measurements, we then organize the H1 variants according to their ability to condense chromatin and produce nucleosome repeat lengths amenable to that compaction. This subtype variation generates a continuum of different chromatin states allowing for fine regulatory control and some overlap in the event one or two subtypes are lost to mutation. We also review the myriad of disparate observations made about each subtype, both somatic and germline specific ones, that lend support to the proposed model. Finally, to demonstrate its adaptability as new data further refines our understanding of H1 subtypes, we show how the model can be applied to experimental observations of telomeric heterochromatin in aging cells.</p>","PeriodicalId":7529,"journal":{"name":"AIMS Biophysics","volume":"2 4","pages":"724-772"},"PeriodicalIF":1.1000,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6615755/pdf/","citationCount":"27","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"AIMS Biophysics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3934/biophy.2015.4.724","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2015/11/16 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 27

Abstract

For the past 50 years, understanding the function of histone H1 heterogeneity has been mired in confusion and contradiction. Part of the reason for this is the lack of a working model that tries to explain the large body of data that has been collected about the H1 subtypes so far. In this review, a global model is described largely based on published data from the author and other researchers over the past 20 years. The intrinsic disorder built into H1 protein structure is discussed to help the reader understand that these histones are multi-conformational and adaptable to interactions with different targets. We discuss the role of each structural section of H1 (as we currently understand it), but we focus on the H1's C-terminal domain and its effect on each subtype's affinity, mobility and compaction of chromatin. We review the multiple ways these characteristics have been measured from circular dichroism to FRAP analysis, which has added to the sometimes contradictory assumptions made about each subtype. Based on a tabulation of these measurements, we then organize the H1 variants according to their ability to condense chromatin and produce nucleosome repeat lengths amenable to that compaction. This subtype variation generates a continuum of different chromatin states allowing for fine regulatory control and some overlap in the event one or two subtypes are lost to mutation. We also review the myriad of disparate observations made about each subtype, both somatic and germline specific ones, that lend support to the proposed model. Finally, to demonstrate its adaptability as new data further refines our understanding of H1 subtypes, we show how the model can be applied to experimental observations of telomeric heterochromatin in aging cells.

Abstract Image

Abstract Image

Abstract Image

组蛋白H1异质性的作用是什么?一个功能模型从50年的谜团中浮现出来。
在过去的50年里,对组蛋白H1异质性功能的理解一直陷入困惑和矛盾之中。部分原因是缺乏一个工作模型来解释迄今为止收集的关于H1亚型的大量数据。在这篇综述中,一个全球模型的描述主要基于作者和其他研究人员在过去20年中发表的数据。讨论了H1蛋白结构中固有的紊乱,以帮助读者理解这些组蛋白是多构象的,并适应与不同靶标的相互作用。我们讨论了H1的每个结构部分的作用(正如我们目前所理解的),但我们关注H1的C末端结构域及其对每个亚型的亲和力、移动性和染色质压实的影响。我们回顾了测量这些特征的多种方法,从圆二色性到FRAP分析,这增加了对每个亚型有时相互矛盾的假设。基于这些测量结果的列表,我们根据H1变体浓缩染色质和产生适合这种压缩的核小体重复长度的能力来组织H1变体。这种亚型变异产生了不同染色质状态的连续体,允许精细的调节控制,并在一个或两个亚型因突变而丢失的情况下出现一些重叠。我们还回顾了对每种亚型的无数不同观察,包括体细胞亚型和种系特异性亚型,这些观察为所提出的模型提供了支持。最后,为了证明其适应性,因为新数据进一步完善了我们对H1亚型的理解,我们展示了该模型如何应用于衰老细胞中端粒异染色质的实验观察。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
AIMS Biophysics
AIMS Biophysics BIOPHYSICS-
CiteScore
2.40
自引率
20.00%
发文量
16
审稿时长
8 weeks
期刊介绍: AIMS Biophysics is an international Open Access journal devoted to publishing peer-reviewed, high quality, original papers in the field of biophysics. We publish the following article types: original research articles, reviews, editorials, letters, and conference reports. AIMS Biophysics welcomes, but not limited to, the papers from the following topics: · Structural biology · Biophysical technology · Bioenergetics · Membrane biophysics · Cellular Biophysics · Electrophysiology · Neuro-Biophysics · Biomechanics · Systems biology
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信