组蛋白H3和H4组装到非洲爪蟾胚胎染色质中的功能结构域。
Functional domains for assembly of histones H3 and H4 into the chromatin of Xenopus embryos.
作者信息
Freeman L, Kurumizaka H, Wolffe A P
机构信息
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2710, USA.
出版信息
Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12780-5. doi: 10.1073/pnas.93.23.12780.
Abstract
Histones H3 and H4 have a well defined structural role in the nucleosome and an established role in the regulation of transcription. We have made use of a microinjection strategy using Xenopus embryos to define the minimal structural components of H3 and H4 necessary for nucleosome assembly into metazoan chromosomes in vivo. We find that both the N-terminal tail of H4, including all sites of acetylation, and the C-terminal alpha-helix of the H4 histone fold domain are dispensable for chromatin assembly. The N-terminal tail and an N-terminal alpha-helix of H3 are also dispensable for chromatin assembly. However, the remainder of the H3 and H4 histone folds are essential for incorporation of these proteins into chromatin. We suggest that elements of the histone fold domain maintain both nucleosomal integrity and have distinct functions essential for cell viability.
摘要
组蛋白H3和H4在核小体中具有明确的结构作用，并且在转录调控中也发挥着既定作用。我们利用非洲爪蟾胚胎的显微注射策略来确定H3和H4的最小结构成分，这些成分是体内核小体组装成后生动物染色体所必需的。我们发现，H4的N端尾巴（包括所有乙酰化位点）以及H4组蛋白折叠结构域的C端α螺旋对于染色质组装都是可有可无的。H3的N端尾巴和N端α螺旋对于染色质组装同样是可有可无的。然而，H3和H4组蛋白折叠的其余部分对于将这些蛋白质整合到染色质中至关重要。我们认为，组蛋白折叠结构域的元件既能维持核小体的完整性，又具有对细胞活力至关重要的独特功能。
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