期刊
JOURNAL OF CELL BIOLOGY
卷 153, 期 7, 页码 1341-1353出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.153.7.1341
关键词
cell fusion; FRAP; histone actetylation; nucleosome; transcription
类别
资金
- Wellcome Trust Funding Source: Medline
Histones H2A and H2B form part of the same nucleosomal structure as H3 and H4. Stable HeLa cell lines expressing histones H2B, H3, and H4 lagged with green fluorescent protein (GFP) were established; the tagged molecules were assembled into nucleosomes. Although H2B-GFP was distributed like DNA, H3-GFP and H4-GFP were concentrated in euchromatin during interphase and in R-bands in mitotic chromosomes.. These differences probably result from an unregulated production of tagged histones and differences in exchange. In both single cells and heterokaryons, photobleaching revealed that H2B-GFP exchanged more rapidly than H3-GFP and H4-GFP. About 3% of H2B exchanged within minutes, whereas similar to 40% did so slowly (t(1/2) similar to 130 min). The rapidly exchanging fraction disappeared in 5,6-dichloro-1-beta -D-ribofuranosylbenzimidazole and so may represent H2B in transcriptionally active chromatin. The slowly exchanging fraction was probably associated with chromatin domains surrounding active units. H3-GFP and H4-GFP were assembled into chromatin when DNA was replicated, and then >80% remained bound permanently. These results reveal that the inner core of the nucleosome is very stable, whereas H2B on the surface of active nucleosomes exchanges continually.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据