Roque Alicia, Ponte Inma, Suau Pedro
Departamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, Spain.
Departamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, Spain.
Biochim Biophys Acta. 2016 Mar;1859(3):444-54. doi: 10.1016/j.bbagrm.2015.09.009. Epub 2015 Sep 28.
H1 linker histones are involved both in the maintenance of higher-order chromatin structure and in gene regulation. Histone H1 exists in multiple isoforms, is evolutionarily variable and undergoes a large variety of post-translational modifications. We review recent progress in the understanding of the folding and structure of histone H1 domains with an emphasis on the interactions with DNA. The importance of intrinsic disorder and hydrophobic interactions in the folding and function of the carboxy-terminal domain (CTD) is discussed. The induction of a molten globule-state in the CTD by macromolecular crowding is also considered. The effects of phosphorylation by cyclin-dependent kinases on the structure of the CTD, as well as on chromatin condensation and oligomerization, are described. We also address the extranuclear functions of histone H1, including the interaction with the β-amyloid peptide.
H1连接组蛋白参与高阶染色质结构的维持和基因调控。组蛋白H1以多种亚型存在，在进化上具有变异性，并经历多种翻译后修饰。我们综述了在理解组蛋白H1结构域折叠和结构方面的最新进展，重点是与DNA的相互作用。讨论了内在无序和疏水相互作用在羧基末端结构域（CTD）折叠和功能中的重要性。还考虑了大分子拥挤对CTD中熔球态的诱导作用。描述了细胞周期蛋白依赖性激酶磷酸化对CTD结构以及染色质凝聚和寡聚化的影响。我们还讨论了组蛋白H1的核外功能，包括与β-淀粉样肽的相互作用。
