The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Relationship between Histone H3 Lysine 9 Methylation, Transcription Repression, and Heterochromatin Protein 1 Recruitment
Open accessAbstract
Histone H3 lysine 9 (H3-K9) methylation has been shown to correlate with transcriptional repression and serve as a specific binding site for heterochromatin protein 1 (HP1). In this study, we investigated the relationship between H3-K9 methylation, transcriptional repression, and HP1 recruitment by comparing the effects of tethering two H3-K9-specific histone methyltransferases, SUV39H1 and G9a, to chromatin on transcription and HP1 recruitment. Although both SUV39H1 and G9a induced H3-K9 methylation and repressed transcription, only SUV39H1 was able to recruit HP1 to chromatin. Targeting HP1 to chromatin required not only K9 methylation but also a direct protein-protein interaction between SUV39H1 and HP1. Targeting methyl-K9 or a HP1-interacting region of SUV39H1 alone to chromatin was not sufficient to recruit HP1. We also demonstrate that methyl-K9 can suppress transcription independently of HP1 through a mechanism involving histone deacetylation. In an effort to understand how H3-K9 methylation led to histone deacetylation in both H3 and H4, we found that H3-K9 methylation inhibited histone acetylation by p300 but not its association with chromatin. Collectively, these data indicate that H3-K9 methylation alone can suppress transcription but is insufficient for HP1 recruitment in the context of chromatin exemplifying the importance of chromatin-associated factors in reading the histone code.
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Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
The language of covalent histone modifications
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The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
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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
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“5A) including a full-length H324K mutant that abolishes enzymatic activity (22, 40), the C-terminal SET domain with or without a H324K mutation, and the N-terminal region that contains the previously identified HP1 interaction domain (the first 39 amino acids) (61) and the CD (SUV C).”
BackgroundRegulation of Heterochromatic Silencing and Histone H3 Lysine-9 Methylation by RNAi
Volpe, T. A., Kidner, C., Hall, I. M., Teng, G., Grewal, S. I. S., & Martienssen, R. A. (2002) · Science · doi:10.1126/science.1074973 · Cited by 2,055
The CBP co-activator is a histone acetyltransferase
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Loss of the Suv39h Histone Methyltransferases Impairs Mammalian Heterochromatin and Genome Stability
Peters, A. H. F. M., O'Carroll, D., Scherthan, H., Mechtler, K., Sauer, S., Schöfer, C., Weipoltshammer, K., Pagani, M., Lachner, M., Kohlmaier, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00542-6 · Cited by 1,766
Cited by
Molecular Signals of Epigenetic States
Bonasio, R., Tu, S., & Reinberg, D. (2010) · Science · doi:10.1126/science.1191078 · Cited by 912
Vakoc, C. R., Mandat, S. A., Olenchock, B. A., & Blobel, G. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.011 · Cited by 696
G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis
Feldman, N., Gerson, A., Fang, J., Li, E., Zhang, Y., Shinkai, Y., Cedar, H., & Bergman, Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1353 · Cited by 651
Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia
Herman, D., Jenssen, K., Burnett, R., Soragni, E., Perlman, S. L., & Gottesfeld, J. M. (2006) · Nature Chemical Biology · doi:10.1038/nchembio815 · Cited by 442
Groner, A. C., Meylan, S., Ciuffi, A., Zangger, N., Ambrosini, G., Dénervaud, N., Bucher, P., & Trono, D. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000869 · Cited by 364
Metadata
- Authors
- Stewart, M. D., Li, J., & Wong, J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-04-01
- Volume
- 25
- Issue
- 7
- Pages
- 2525-2538
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2104870341
- Cited by
- 351
- References
- 65
- FWCI
- 10.83
- Type
- journal article
- Language
- en
- Open access
- green
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