The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Histone H3 Lysine 4 Methylation Disrupts Binding of Nucleosome Remodeling and Deacetylase (NuRD) Repressor Complex
Open accessAbstract
Histone N-terminal tails are post-translationally modified in many ways. At lysine residues, histones can be either acetylated or methylated. Both modifications lead to the binding of specific proteins; bromodomain proteins, such as GCN5, bind acetyl lysines and the chromodomain protein, HP1, binds methyl lysine 9 of histone H3. Here we show that the previously characterized transcriptional repressor complex NuRD (nucleosome remodeling and deacetylase) binds to the histone H3 N-terminal tail and that methylation at lysine 4, but not lysine 9, prevents binding. Given that lysine 4 methylation is found at sites of active transcription, these results suggest that a function of lysine 4 methylation is to disrupt the association of histones with a repressor complex.
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Citations
Cites
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
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Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
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Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
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Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
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The Occurrence of iε-N-Methyl Lysine in Histones
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Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin
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Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Self-citationHistone and chromatin cross-talk
Fischle, W., Wang, Y., & Allis, C. D. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00013-9 · Cited by 1,207
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Turner, B. M. (2002) · Cell · doi:10.1016/s0092-8674(02)01080-2 · Cited by 1,142
The many faces of histone lysine methylation
Lachner, M., & Jenuwein, T. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00335-6 · Cited by 819
Elongation by RNA polymerase II: the short and long of it
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Metadata
- Authors
- Zegerman, P., Canas, B., Pappin, D., & Kouzarides, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 277
- Issue
- 14
- Pages
- 11621-11624
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2097836350
- Cited by
- 247
- References
- 9
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
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