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Histone H2A/H2B Dimer Exchange by ATP-Dependent Chromatin Remodeling Activities
Open accessAbstract
Summary Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodelling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best characterised chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome Assembly Proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein cross-linking we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone mediated lysine acetylation. This alternate mode of histone interaction also provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.
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Citations
Cites
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447
Cited by
The Biology of Chromatin Remodeling Complexes
Clapier, C. R., & Cairns, B. R. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062706.153223 · Cited by 2,380
Epigenetics: The link between nature and nurture
Tammen, S. A., Friso, S., & Choi, S.-W. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.07.018 · Cited by 494
Histone dynamics in living cells revealed by photobleaching
Kimura, H. (2005) · DNA Repair · doi:10.1016/j.dnarep.2005.04.012 · Cited by 109
Two Chromatin Remodeling Activities Cooperate during Activation of Hormone Responsive Promoters
Vicent, G. P., Zaurin, R., Nacht, A. S., Li, A., Font-Mateu, J., Le Dily, F., Vermeulen, M., Mann, M., & Beato, M. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000567 · Cited by 55
Metadata
- Authors
- Bruno, M., Flaus, A., Stockdale, C., Rencurel, C., Ferreira, H., & Owen-Hughes, T.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 12
- Issue
- 6
- Pages
- 1599-1606
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1968177936
- Cited by
- 195
- References
- 1
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Bruno, M., Flaus, A., Stockdale, C., Rencurel, C., Ferreira, H., & Owen-Hughes, T. (2003). Histone H2A/H2B Dimer Exchange by ATP-Dependent Chromatin Remodeling Activities. Molecular Cell. https://doi.org/10.1016/s1097-2765(03)00499-4
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
