Cell
Volume 72, Issue 1, 15 January 1993, Pages 73-84
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Article
A positive role for histone acetylation in transcription factor access to nucleosomal DNA

https://doi.org/10.1016/0092-8674(93)90051-QGet rights and content

Abstract

Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFIIIA of the 5S RNA gene within model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones also facilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restricting transcription factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules.

References (75)

  • P.S. Kayne et al.

    Extremely conserved histone H4 N terminus is dispensible for growth but essential for repressing the silent mating loci in yeast

    Cell

    (1988)
  • X. Liao et al.

    Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene

    J. Mol. Biol.

    (1992)
  • K.W. Marvin et al.

    Isolation and characterization of acetylated histones H3/H4 and their assembly into nucleosomes

    J. Biol. Chem.

    (1990)
  • V.G. Norton et al.

    Histone acetylation reduces nucleosome core particle linking number change

    Cell

    (1989)
  • V.G. Norton et al.

    Nucleosome linking number change controlled by acetylation of histones H3 and H4

    J. Biol. Chem.

    (1990)
  • M. Perry et al.

    The effect of histone hyperacetylation on the nuclease sensitivity and the solubility of chromatin

    J. Biol. Chem.

    (1981)
  • B. Piña et al.

    Nucleosome positioning modulates accessibility of regulatory proteins to the mouse mammary tumor virus promoter

    Cell

    (1990)
  • M. Roberge et al.

    Inhibition of 5S RNA transcription in vitro by nucleosome cores with low or high levels of histone acetylation

    FEBS Lett.

    (1991)
  • S. Sakonju et al.

    Contact points between a positive transcription factor and the Xenopus 5S RNA gene

    Cell

    (1982)
  • R.T. Simpson

    Nucleosome positioning: occurrence, mechanisms and functional consequences

    Nucl. Acids Res.

    (1991)
  • D.R. Smith et al.

    Domains of the positive transcription factor specific for the Xenopus 5S RNA gene

    Cell

    (1984)
  • D. Tremethick et al.

    The transcription complex of the 5S RNA gene, but not transcription factor TFIIIA alone, prevents nucleosomal repression of transcription

    J. Biol. Chem.

    (1990)
  • B.M. Turner et al.

    Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei

    Cell

    (1992)
  • J. Walker et al.

    Affinity chromatography of mammalian and yeast nucleosomes

    J. Biol. Chem.

    (1990)
  • J.H. White et al.

    Effect of nucleosome distortion on the linking deficiency in relaxed minichromosomes

    J. Mol. Biol.

    (1989)
  • M. Whiteway et al.

    The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways

    Cell

    (1985)
  • J.P. Whitlock et al.

    Localization of the sites along nucleosomal DNA which interact with NH2-terminal histone regions

    J. Biol. Chem.

    (1977)
  • A.P. Wolffe et al.

    Differential 5S RNA gene expression in vitro

    Cell

    (1987)
  • A.P. Wolffe et al.

    A bacteriophage RNA polymerase transcribes through a Xenopus 5S RNA gene transcription complex without disrupting it

    Cell

    (1986)
  • W. Wray et al.

    Silver staining of proteins in polyacrylamide gels

    Anal. Biochem.

    (1981)
  • A. Zweidler

    Resolution of histones by polyacrylamide gel electrophoresis in the presence of nonionic detergent

    Meth. Cell Biol.

    (1978)
  • V. Allfrey et al.

    Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis

  • G. Almouzni et al.

    Transcription complex disruption caused by a transition in chromatin structure

    Mol. Cell. Biol.

    (1991)
  • T.K. Archer et al.

    Transcription factor access is mediated by accurately positioned nucleosomes on the mouse mammary tumor virus promoter

    Mol. Cell. Biol.

    (1991)
  • J. Ausio et al.

    Histone hyperacetylation: its effects on nucleosome conformation and stability

    Biochemistry

    (1986)
  • B.W. Baer et al.

    Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes

    Nature

    (1983)
  • L. Böhm et al.

    Proteases as structural probes for chromatin: the domain structure of histones

    Biosci. Rep.

    (1984)
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