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Published online 18 June 2001. doi:10.1083/jcb.153.7.1341
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© The Rockefeller University Press, 0021-9525/2001/6/1341/ $5.00
The Journal of Cell Biology, Volume 153, Number 7, June 25, 2001 1341-1354

Original Article

Kinetics of Core Histones in Living Human Cells: Little Exchange of H3 and H4 and Some Rapid Exchange of H2B

Hiroshi Kimuraa and Peter R. Cooka
a Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom

Correspondence to: Peter R. Cook, Sir William Dunn School of Pathology, University of Oxford, South Parks Rd., Oxford OX1 3RE, UK. Tel:44-1865-275528 Fax:44-1865-275515 E-mail:peter.cook{at}path.ox.ac.uk.

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 tagged 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 ~40% did so slowly (t1/2 ~ 130 min). The rapidly exchanging fraction disappeared in 5,6-dichloro-1-ß-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.

Key Words: cell fusion, FRAP, histone actetylation, nucleosome, transcription


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