Abstract
In prokaryotic organisms (eg. bacteria such as E.Coli), genes are switched on and off in response to environmental signals, such as the availability, or otherwise, of nutrients. E.coli has only a single RNA polymerase that is directed towards particular genes by association with ancilliary proteins, called sigma factors, which confer upon it the ability to recognise DNA sequences in the promotors of these genes. By changing the availability of these factors and of other regulators in response to environmental cues, bacteria are able to maintain an appropriate pattern of gene expression. In recent years it has been shown that eukaryotic organisms also use ancilliary, DNA-binding proteins, generally called Transcription Factors, to regulate transcription of specific genes. However, it has also become clear that the transcription of eukaryotic genes always requires complex assemblies of several different proteins in addition to RNA polymerase. Protein-protein as well as protein-DNA interactions are of crucial importance in transcription.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Reference
Chromatin and histone modifications
Van Holde, K. (1989)Chromatin. Springer-Verlag, New York.
Wu, R.S., Panusz, H.T., Hatch, C.L. and Bonner, W.M. (1984) Histones and their modifications. In:CRC Critical Reviews of Biochemistryvol.20, pp.201–263.
Reviews of histone acetylation
Csordas, A. (1990) On the biological role of histone acetylation.Biochem. J.26523–38.
Loidl, P. (1994) Histone acetylation: facts and questions.Chromosoma 103, 441–449.
Turner, B.M. (1991) Histone acetylation and control of gene expression.J. Cell Sci.9913–20.
Turner, B.M. and O’Neill, L.P. (1995) Histone acetylation in chromatin and chromosomes.Sem.Cell Biol.6229–236.
DNA replication and chromatin assembly
Jackson, V., Shires, A., Tanphaichitr, N. and Chalkley, R. (1976) Modifications to histones immediately after synthesis.J.Mol.Biol.104471–483.
Kaufman, P.D., Kobayashi, R., Kessler, N. and Stillman, B. (1995) The p150 and p60 subunits of chromatin assembly factor 1: a molecular link between newly synthesized histones and DNA replication.Cell 81, 1105–1114.
Laskey, R.A., Mills, A.D., Philpott, A., Leno, G.H., Dilworth, S.M. and Dingwall, C. (1993) The role of nucleoplasmin in chromatin assembly and disassembly.Phil.Trans.Roy.Soc B.339263–269.
Sobel, R.E., Cook, R.G., Perry, C.A., Annunziato, A.T., Allis, C.D. (1995) Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4.Proc.Natl.Acad.Sci. USA 92, 1237–1241.
Cell cycle progression
Bradbury, M. (1992) Reversible histone modifications and the chromosome cell cycle.BioEssays 14, 9–16.
Megee, P.C., Morgan, B.A. and Smith, M.M. (1995) Histone H4 and the maintenance of genome integrity.Genes Dev.91716–1727.
Transcription
Braunstein M., Rose, A.B., Holmes, S.G., Allis, C.D. and Broach, J.R. (1993) Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.GenesDev.7, 592–604.
Hebbes, T.R., Clayton, A.L., Thorne, A.W., Crane-Robinson, C. (1994) Core histone hyperacetylation co-maps with generalized DNasel sensitivity in the chicken 11-globin chromosomal domain.EMBO J.131823–1830
Lee, D.Y., Hayes, J.J., Pruss, D. and Wolffe, A.P. (1993) A postive role for histone acetylation in transcription factor access to nucleosomal DNA.Cell 72, 73–84.
O’Neill, L.P. and Turner, B.M. (1995) Histone H4 acetylation distinguishes coding regions of the genome from heterochromatin in a differentiation-dependent but transcription-independent manner.EMBO J.143946–3957.
Perry, M. and Chalkley, R. (1982) Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin.J.BioLChem.2577336–7347.
Thompson, J.S., Ling, X. and Grunstein, M. (1994) Histone H3 amino terminus is required for telomeric and silent mating locus repression in yeast.Nature 369, 245–247
Vettesse-Dadey, M., Walter, P., Chen, H., Juan, L-J. and Workman, J.L. (1994) Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores.Mol.Cell.Biol.14970–981.
Genomic marking
Botte, J.R., Lavender, J.S., Richman, R., Palmer, M.J., Turner, B.M. and Kuroda, M.I. (1994) Acetylated histone H4 on the male X chromosome is associated with dosage compensation inDrosophila. Genes Dev.896–104.
Jeppesen, P. and Turner, B.M. (1993) The inactive X chromosome in female mammals is distinguished by lack of histone H4 acetylation, a marker for gene expression.Cell 74, 281–289.
Turner, B.M., Birley, A.J. and Lavender, J. (1992) Histone 114 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains inDrosophilapolytene nuclei.Cell 69, 375–384
Histone-binding and nucleosome signalling
Edmondson, D.G., Smith, M.M. and Roth, S.Y. (1996) Repression domain of the yeast global repressor Tupl interacts directly with histones H3 and H4.Genes Dev.101247–1259
Hecht, A., Laroche, T., Strahl-Bosinger, S., Gasser, S.M. and Grunstein, M. (1995) Histone H3 and H4 N-termini interact with the Silent Information Regulators Sir3 and Sir4: a molecular model for the formation of heterochromatin in yeast.Cell 80, 583–592.
Johnson, L.M., Kayne, P.S., Kahn, E.S. and Grunstein, M. (1990) Genetic evidence for an interaction between S1R3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae.Proc.NutL.Acad.Sci. USA.876286–6290.
Turner, B.M. (1993) Decoding the nucleosome.Cell.755–8.
Wolfe, A.P. and Pruss, D. (1996) Chromatin: Hanging on to histones.Current Biol.6234–237.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Turner, B.M. (1997). Histone Acetylation. In: Nicolini, C. (eds) Genome Structure and Function. NATO ASI Series, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5550-2_8
Download citation
DOI: https://doi.org/10.1007/978-94-011-5550-2_8
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6338-8
Online ISBN: 978-94-011-5550-2
eBook Packages: Springer Book Archive