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Cited by 675Genomics and Chromatin DynamicsNuclear Structure and FunctionChromatin Remodeling and Cancer

Kinetics of Core Histones in Living Human Cells

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Kimura, Hiroshi, Cook, Peter R.·2001·The Journal of Cell Biology
DOI 10.1083/jcb.153.7.1341PMC PMC2150718
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Abstract

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 approximately 40% did so slowly (t(1/2) approximately 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.

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  • The mobility of Stat1 is much faster than core histones and similar to other inducible transcriptional regulators.

    “Compared with other studies, the mobility of Stat1 was much faster than the core histones and similar to other inducible transcriptional regulators (McNally et al. 2000; Kimura and Cook 2001; Lillemeier et al. 2001).”

    From DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1 (2003) · cites this paper as Kimura and Cook 2001

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Authors
Kimura, H., & Cook, P. R.
Affiliations
  • aSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom
  • University of Oxford (GB)
ORCID
Cook, Peter R.
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2001-06-18
Volume
153
Issue
7
Pages
1341-1354
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.153.7.1341
PMC
PMC2150718
OpenAlex
W2143351999
Cited by
675
References
1
Citations by year
2026: 14 · 2025: 11 · 2024: 21 · 2023: 25 · 2022: 12 · 2021: 32 · 2020: 29 · 2019: 23 · 2018: 17 · 2017: 17 · 2016: 30 · 2015: 28 · 2014: 20 · 2013: 27 · 2012: 19
FWCI
12.36
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
Keywords
histone H2B, histone H3, histone H4, nucleosome, euchromatin, R-band, metaphase chromosomes, heterokaryons, photobleaching, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole, chromatin replication, transcriptionally active chromatin, nucleosome stability
MeSH terms
Cell Line, Cell Nucleus, Chromatin, Chromosomes, Dichlororibofuranosylbenzimidazole, DNA, HeLa Cells, Histones, Humans, Kinetics, Luminescent Proteins, Microscopy, Fluorescence, Nucleosomes, Photochemistry, Protein Binding, Recombinant Fusion Proteins, Transfection, S Phase, Macromolecular Substances, Green Fluorescent Proteins

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