Protein modules that manipulate histone tails for chromatin regulation (original) (raw)

• Wolffe, A. P. Chromatin: Structure and Function (Academic Press, London, 1992).
  Google Scholar
• Allfrey, V. G., Faulkner, R. & Mirsky, A. E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl Acad. Sci. USA 51, 786–794 (1964).
  Article CAS PubMed PubMed Central Google Scholar
• Bradbury, E. M. Reversible histone modifications and the chromosome cell cycle. BioEssays 14, 9–16 (1992).
  Article CAS PubMed Google Scholar
• Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389, 349–352 (1997).
  Article CAS PubMed Google Scholar
• Thompson, J. S., Ling, X. & Grunstein, M. Histone H3 amino terminus is required for telomeric and silent mating locus repression in yeast. Nature 369, 245–247 (1994).
  Article CAS PubMed Google Scholar
• Durrin, L., Mann, R., Kayne, P. & Grunstein, M. Yeast histone H4 N–terminal sequence is required for promoter activation in vivo. Cell 65, 1023–1031 (1991).
  Article CAS PubMed Google Scholar
• Wolffe, A. P. & Hayes, J. J. Chromatin disruption and modification. Nucleic Acids Res. 27, 711–720 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Morales, V. & Richard-Foy, H. Role of histone N-terminal tails and their acetylation in nucleosome dynamics. Mol. Cell. Biol. 20, 7230–7237 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Hansen, J. C., Tse, C. & Wolffe, A. P. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37, 17637–17641 (1998).
  Article CAS PubMed Google Scholar
• Sivolob, A., De Lucia, F., Alilat, M. & Prunell, A. Nucleosome dynamics. VI. Histone tail regulation of tetrasome chiral transition. A relaxation study of tetrasomes on DNA minicircles. J. Mol. Biol. 295, 55–69 (2000).
  Article CAS PubMed Google Scholar
• Wang, X., Moore, S. C., Laszckzak, M. & Ausio, J. Acetylation increases the α-helical content of the histone tails of the nucleosome. J. Biol. Chem. 275, 35013–35020 (2000).
  Article CAS PubMed Google Scholar
• Mutskov, V. et al. Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding. Mol. Cell. Biol. 18, 6293–6304 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Polach, K. J., Lowary, P. T. & Widom, J. Effects of core histone tail domains on the equilibrium constants for dynamic DNA site accessibility in nucleosomes. J. Mol. Biol. 298, 211–223 (2000).
  Article CAS PubMed Google Scholar
• Turner, B. M. Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell. Mol. Life Sci. 54, 21–31 (1998).The first to suggest that histone tail modifications may be histone marks that signal downstream transcriptional events.
  Article CAS PubMed Google Scholar
• Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41–45 (2000).Builds on the initial proposal of Turner, to propose that distinct histone tail modifications provide a 'histone code' for downstream transcriptional activities.
  Article CAS PubMed Google Scholar
• Georgakopoulos, T. & Thireos, G. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11, 4145–4152 (1992).
  Article CAS PubMed PubMed Central Google Scholar
• Marcus, G., Silverman, N., Berger, S., Horiuchi, J. & Guarente, L. Functional similarity and physical association between GCN5 and ADA2-putative transcriptional adaptors. EMBO J. 13, 4807–4815 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Horiuchi, J., Silverman, N., Marcus, G. A. & Guarente, L. ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Mol. Cell. Biol. 15, 1203–1209 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Candau, R. & Berger, S. L. Structural and functional analysis of yeast putative adaptors: evidence for an adaptor complex in vivo. J. Biol. Chem. 271, 5237–5345 (1996).
  Article CAS PubMed Google Scholar
• Barlev, N. A. et al. Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein. J. Biol. Chem. 270, 19337–19344 (1995).
  Article CAS PubMed Google Scholar
• Silverman, N., Agapite, J. & Guarente, L. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. Proc. Natl Acad. Sci. USA 91, 11665–11668 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Zamir, I. et al. A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains. Mol. Cell. Biol. 16, 5458–5465 (1996).
  Article CAS PubMed PubMed Central Google Scholar
• Horlein, A. J. et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377, 397–404 (1995).
  Article CAS PubMed Google Scholar
• Kurokawa, R. et al. Polarity-specific activities of retinoic acid receptors determined by a co-repressor. Nature 377, 451–454 (1995).
  Article CAS PubMed Google Scholar
• Heinzel, T. et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387, 43–48 (1997).
  Article CAS PubMed Google Scholar
• Alland, L. et al. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387, 49–55 (1997).
  Article CAS PubMed Google Scholar
• Pogo, B. G. T., Allfrey, V. G. & Mirsky, A. E. RNA synthesis and histone acetylation during the course of gene activation in lymphocytes. Proc. Natl Acad. Sci. USA 55, 6212–6222 (1966).
  Article Google Scholar
• Vidali, G., Boffa, L. C., Bradbury, E. M. & Allfrey, V. G. Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNAase I sensitivity of the associated DNA sequences. Proc. Natl Acad. Sci. USA 75, 2239–2243 (1978).
  Article CAS PubMed PubMed Central Google Scholar
• Hebbes, T. R., Thorne, A. W. & Crane-Robinson, C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7, 1395–1403 (1988).
  Article CAS PubMed PubMed Central Google Scholar
• Hebbes, T. R., Clayton A. L., Throne A. W. & Crane-Robinson, C. Core histone hyperacetylation co-maps with generalized DNase I sensitivity in the chicken β-globin chromosomal domain. EMBO J. 13, 1823–1830 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Vettese-Dadey, M. et al. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J 15, 2508–2518 (1996).
  Article CAS PubMed PubMed Central Google Scholar
• Sealy, L. & Chalkley, R. DNA associated with hyperacetylated histone is preferentially digested by DNase I. Nucleic Acids Res. 5, 1863–1876 (1978).
  Article CAS PubMed PubMed Central Google Scholar
• Brownell, J. E. et al. Tetrahymena histone acetyltransferase A: a homolog of yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843–851 (1996).The first to functionally link gene activation by a transcriptional co-activator to the histone acetyltransferase activity of that co-activator.
  Article CAS PubMed Google Scholar
• Berger, S. L. et al. Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains. Cell 70, 251–265 (1992).
  Article CAS PubMed Google Scholar
• Wang, L., Liu, L. & Berger, S. L. Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev. 12, 640–653 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Kuo, M. H., Zhou, J. X., Jambeck, P., Churchill, M. E. A. & Allis, C. D. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. Genes Dev. 12, 627–639 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Shikama, N., Lyon, J. & LaThangue, N. B. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7, 230–236 (1997).
  Article CAS Google Scholar
• Bannister, A. J. & Kouzarides, T. The CBP co-activator is a histone acetyltransferase. Nature 384, 641–643 (1996).
  Article CAS PubMed Google Scholar
• Mizzen, C. A. et al. The TAFII250 subunit of TFIID has histone acetyltransferase activity. Cell 87, 1261–1270 (1996).
  Article CAS PubMed Google Scholar
• Cress, W. D. & Seto, E. Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol. 184, 1–16 (2000).
  Article CAS PubMed Google Scholar
• Kuo, M. H. & Allis, C. D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20, 615–626 (1998).
  Article CAS PubMed Google Scholar
• Neal, K. C., Pannuti, A., Smith, E. R. & Lucchesi, J. C. A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF. Biochim. Biophys. Acta1490, 170–174 (2000).
  Article CAS Google Scholar
• Sterner, D. E. & Berger, S. L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64, 435–459 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Kawasaki, H. et al. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 405, 195–200 (2000).
  Article CAS PubMed Google Scholar
• Takechi, S. & Nakayama, T. Sas3 is a histone acetyltransferase and requires a zinc finger motif. Biochem. Biophys. Res. Commun. 266, 405–410 (1999).
  Article CAS PubMed Google Scholar
• EhrenhoferMurray, A. E., Rivier, D. H. & Rine, J. The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function. Genetics 145, 923–934 (1997).
  CAS Google Scholar
• Kuo, M. H. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269–272 (1996).
  Article CAS PubMed Google Scholar
• Trievel, R. C., Li, F.-Y. & Marmorstein, R. Application of a novel fluorescence histone acetyltransferase enzyme assay to study the substrate specificity of human PCAF. Anal. Biochem. 287, 319–328 (2000).
  Article CAS PubMed Google Scholar
• John, S. et al. The Something About Silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAFII30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)–FACT complex. Genes Dev. 14, 1196–1208 (2000).
  CAS PubMed PubMed Central Google Scholar
• Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H. & Nakatani, Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87, 953–959 (1996).
  Article CAS PubMed Google Scholar
• Grant, P. A. et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11, 1640–1650 (1997).
  Article CAS PubMed Google Scholar
• Allard, S. et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 18, 5108–5119 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Grant, P. A. et al. Expanded lysine acetylation specificity of Gcn5 in native complexes. J. Biol. Chem. 274, 5895–5900 (1999).
  Article CAS PubMed Google Scholar
• Trievel, R. C. et al. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl Acad. Sci. USA 96, 8931–8936 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Clements, A. et al. Crystal structure of the histone acetyltransferase domain of the human P/CAF transcriptional regulator bound to coenzyme-A. EMBO J. 18, 3521–3532 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Rojas, J. R. et al. Structure of the Tetrahymena GCN5 bound to coenzyme-A and a histone H3 peptide. Nature 401, 93–98 (1999).Revealed the first high-resolution structure of a HAT bound to a histone peptide substrate.
  Article CAS PubMed Google Scholar
• Lin, Y., Fletcher, C. M., Zhou, J., Allis, C. D. & Wagner, G. Solution structure of the catalytic domain of Tetrahymena GCN5 histone acetyltransferase in complex with coenzyme A. Nature 400, 86–89 (1999).
  Article CAS PubMed Google Scholar
• Yan, Y., Barlev, N. A., Haley, R. H., Berger, S. L. & Marmorstein, R. Crystal structure of yeast Esa1 suggests a unified mechanism of catalysis and substrate binding by histone acetyltransferases. Mol. Cell 6, 1195–1205 (2000).
  Article CAS PubMed Google Scholar
• Dutnall, R. N., Tafrov, S. T., Sternglanz, R. & Ramakrishnan, V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94, 427–438 (1998).
  Article CAS PubMed Google Scholar
• Jeanmougin, F., Wurtz, J. M., LeDouarin, B., Chambon, P. & Losson, R. The bromodomain revisited. Trends Biochem. Sci. 22, 151–153 (1997).
  Article CAS PubMed Google Scholar
• Winston, F. & Allis, C. D. The bromodomain: a chromatin-targeting module? Nature Struct. Biol. 6, 601–604 (1999).
  Article CAS PubMed Google Scholar
• Sterner, D. E. et al. Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction. Mol. Cell. Biol. 19, 86–98 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Kraus, W. L., Manning, E. T. & Kadonaga, J. T. Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates. Mol. Cell. Biol. 19, 8123–8135 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Du, J., Nasir, I., Benton, B. K., Kladde, M. P. & Laurent, B. C. Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins. Genetics 150, 987–1005 (1998).
  CAS PubMed PubMed Central Google Scholar
• Matangkasombut, O., Buratowski, R. M., Swilling, N. W. & Buratowski, S. Bromodomain factor 1 corresponds to a missing piece of yeast TFIID. Genes Dev 14, 951–962 (2000).
  CAS PubMed PubMed Central Google Scholar
• Ornaghi, P., Ballario, P., Lena, A. M., Gonzalez, A. & Filetici, P. The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. J. Mol. Biol. 287, 1–7 (1999).
  Article CAS PubMed Google Scholar
• Dhalluin, C. et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399, 491–496 (1999).Provided the first evidence that bromodomains specifically target acetyl-lysine-containing histone substrates.
  Article CAS PubMed Google Scholar
• Jacobson, R. H., Ladurner, A. G., King, D. S. & Tjian, R. Structure and function of a human TAFII250 double bromodomain module. Science 288, 1422–1425 (2000).
  Article CAS PubMed Google Scholar
• Owen, D. J. et al. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p. EMBO J. 19, 6141–6149 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Clayton, A. L., Rose, S., Barratt, M. J. & Mahadevan, L. C. Phosphoacetylation of histone H3 on c_-fos_- and c_-jun_-associated nucleosomes upon gene activation. EMBO J. 19, 3714–3726 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Nowak, S. J. & Corces, V. G. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Dev. 14, 3003–3013 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Cheung, P. et al. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5, 905–915 (2000).
  Article CAS PubMed Google Scholar
• Lo, W. -S. et al. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell 5, 917–926 (2000).References 72 and 73 revealed that Ser10 phosphorylation of histone H3 is functionally linked to histone acetylation at Lys14 and to gene activation of a subset of Gcn5-dependent genes.
  Article CAS PubMed Google Scholar
• Hsu, J. Y. et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/Aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102, 279–291 (2000).
  Article CAS PubMed Google Scholar
• De Souza, C. P., Osmani, A. H., Wu, L. P., Spotts, J. L. & Osmani, S. A. Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans. Cell 102, 293–302 (2000).References 74 and 75 indicate that phosphorylation of histone H3 at Ser 10 is mediated by the Ipl1/Aurora kinase and that this activity is functionally linked to chromosome condensation during mitosis.
  Article CAS PubMed Google Scholar
• Hassan, A. H., Neely, K. E. & Workman, J. L. Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes. Cell 104, 817–827 (2001).
  Article CAS PubMed Google Scholar
• Cosma, M. P., Tanaka, T. & Nasmyth, K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell 97, 299–311 (1999).
  Article CAS PubMed Google Scholar
• Krebs, J. E., Fry, C. J., Samuels, M. L. & Peterson, C. L. Global role for chromatin remodeling enzymes in mitotic gene expression. Cell 102, 587–598 (2000).References 76 – 78 indicate a functional link between histone acetylation and chromatin remodelling.
  Article CAS PubMed Google Scholar
• Weiler, K. S. & Wakimoto, B. T. Heterochromatin and gene expression in Drosophila. Annu. Rev. Genet. 29, 577–605 (1995).
  Article CAS PubMed Google Scholar
• Grunstein, M. Molecular model for telomeric heterochromatin in yeast. Curr. Opin. Cell Biol. 9, 383–387 (1997).
  Article CAS PubMed Google Scholar
• Reuter, G. & Spierer, P. Position effect variegation and chromatin proteins. Bioessays 14, 605–612 (1992).
  Article CAS PubMed Google Scholar
• Allshire, R. C., Nimmo, E. R., Ekwall, K., Javerzat, J. P. & Cranston, G. Mutations derepressing silent centromeric domains in fission yeast disrupt chromosome segregation. Genes Dev. 9, 218–233 (1995).
  Article CAS PubMed Google Scholar
• Schotta, G. & Reuter, G. Controlled expression of tagged proteins in Drosophila using a new modular P-element vector system. Mol. Gen. Genet. 262, 916–920 (2000).
  Article CAS PubMed Google Scholar
• Tschiersch, B. et al. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes. EMBO J. 13, 3822–3831 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593–599 (2000).Shows that suppressors of variegation gene product, Su(var)3–9, mediates gene silencing through its histone H3 methyltransferase activity.
  Article CAS PubMed Google Scholar
• Jenuwein, T., Laible, G., Dorn, R. & Reuter, G. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell. Mol. Life Sci. 54, 80–93 (1998).
  Article CAS PubMed Google Scholar
• Bannister, A. J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 401, 120–124 (2001).
  Article Google Scholar
• Lachner, M., O'Carroll, D., Rea, S., Mechtler, K. & Jenuwein, T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 401, 116–120 (2001).References 87 and 88 indicate that the chromodomain of the heterochromatin-associated protein, HP1, targets the Lys9 of histone H3 for heterochromatin assembly and gene silencing.
  Article Google Scholar
• Eissenberg, J. C. et al. Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster. Proc. Natl Acad. Sci. USA 87, 9923–9927 (1990).
  Article CAS PubMed PubMed Central Google Scholar
• Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D. & Grewal, S. I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292, 110–113 (2001).
  Article CAS PubMed Google Scholar
• Akhtar, A., Zink, D. & Becker, P. B. Chromodomains are protein–RNA interaction modules. Nature 407, 405–409 (2000).
  Article CAS PubMed Google Scholar
• Ball, L. J. et al. Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. EMBO J. 16, 2473–2481 (1997).Provides the first atomic structure of a chromodomain.
  Article CAS PubMed PubMed Central Google Scholar
• Platero, J. S., Hartnett, T. & Eissenberg, J. C. Functional analysis of the chromo domain of HP1. EMBO J. 14, 3977–3986 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Edmondson, S. P., Qiu, L. & Shriver, J. W. Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry 34, 13289–133304 (1995).
  Article CAS PubMed Google Scholar
• Baumann, H., Knapp, S., Lundback, T., Ladenstein, R. & Hard, T. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nature Struct. Biol. 1, 808–819 (1994).
  Article CAS PubMed Google Scholar
• Aasland, R. & Stewart, A. F. The chrome shadow domain, a second chrome domain in heterochromatin-binding protein-1, HP1. Nucleic Acids Res. 23, 3168–3173 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Fanti, L., Giovinazzo, G., Berloco, M. & Pimpinelli, S. The heterochromatin protein 1 prevents telomere fusions in Drosophila. Mol. Cell 2, 527–538 (1998).
  Article CAS PubMed Google Scholar
• Murzina, N., Verreault, A., Laue, E. & Stillman, B. Heterochomatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. Mol. Cell 4, 529–540 (1999).
  Article CAS PubMed Google Scholar
• Smothers, J. F. & Henikoff, S. The HP1 chromo shadow domain binds a consensus peptide pentamer. Curr. Biol. 10, 27–30 (2000).
  Article CAS PubMed Google Scholar
• Brasher, S. V. et al. The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chrome domain dimer. EMBO J. 19, 1587–1597 (2000).Provides the first atomic structure of a chromoshadow domain.
  Article CAS PubMed PubMed Central Google Scholar
• Strahl, B. D., Ohba, R., Cook, R. G. & Allis, C. D. Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc. Natl Acad. Sci. USA 96, 14967–14972 (1999).Indicates that histone methylation can be correlated with gene activation.
  Article CAS PubMed PubMed Central Google Scholar
• Chen, D. et al. Regulation of transcription by a protein methyltransferase. Science 284, 2174–2177 (1999).
  Article CAS PubMed Google Scholar
• Stallcup, M. R. et al. Co-operation between protein-acetylating and protein-methylating co-activators in transcriptional activation. Biochem. Soc. Trans. 28, 415–418 (2000).
  Article CAS PubMed Google Scholar
• Travers, A. An engine for nucleosome remodeling. Cell 96, 311–314 (1999).
  Article CAS PubMed Google Scholar
• Carlson, M. & Laurent, B. C. The SNF/SWI family of global transcriptional activators. Curr. Opin. Cell Biol. 6, 396–402 (1994).
  Article CAS PubMed Google Scholar
• Peterson, C. L. & Tamkun, J. W. The SWI–SNF complex: a chromatin remodeling machine? Trends Biochem. Sci. 20, 143–146 (1995).
  Article CAS PubMed Google Scholar
• Ng, H. H. & Bird, A. Histone deacetylases: silencers for hire. Trends Biochem. Sci. 25, 121–126 (2000).
  Article CAS PubMed Google Scholar
• Kouzarides, T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet. Dev. 9, 40–48 (1999).
  Article CAS PubMed Google Scholar
• Xue, Y. et al. NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol. Cell 2, 851–861 (1998).Describes a transcriptional regulatory complex that has both histone deacetylase and chromatin remodelling activity, indicating a direct link between the histone acetylation status and chromatin remodelling.
  Article CAS PubMed Google Scholar
• Borden, K. L. RING domains: master builders of molecular scaffolds? J. Mol. Biol. 295, 1103–1112 (2000).
  Article CAS PubMed Google Scholar
• Aasland, R., Gibson, T. J. & Stewart, A. F. The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem. Sci. 20, 56–59 (1995).
  Article CAS PubMed Google Scholar
• Jackson, P. K. et al. The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases. Trends Cell Biol. 10, 429–439 (2000).
  Article CAS PubMed Google Scholar
• Aasland, R., Stewart, A. F. & Gibson, T. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional corepressor N-CoR and TFIIIB. Trends Biochem. Sci. 21, 87–88 (1996).
  CAS PubMed Google Scholar
• Sullivan, S. A., Aravind, L., Makalowski, I., Baxevanis, A. D. & Landsman, D. The histone database: a comprehensive WWW resource for histones and histone fold-containing proteins. Nucleic Acids Res. 28, 320–322 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Burley, S. K. & Roeder, R. G. Biochemistry and structural biology of transcription factor IID (TFIID). Annu. Rev. Biochem. 65, 769–799 (1996).
  Article CAS PubMed Google Scholar
• Xie, X. et al. Structural similarity between TAFs and the heterotetrameric core of the histone octamer. Nature 380, 316–322 (1996).
  Article CAS PubMed Google Scholar
• Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 angstrom resolution. Nature 389, 251–260 (1997).Describes the atomic structure of the nucleosome core particle indicating that, at least in the context of the core particle, the histone tail regions are largely disordered.
  Article CAS PubMed Google Scholar