Nucleic Acids Research, 1990, Vol. 18, No. 9 2739-2747
© 1990
Molecular Biology |
Histone hyperacetylation can induce unfolding of the nucleosome core particle
Department of Medical Biochemistry, Faculty of Medicine, University of Calgary 3330 Hospital Dr.NW, Calgary, Alberta T2N 4N1, Canada
Received December 6, 1989. Accepted February 12, 1990.
A direct correlation exists between the level of histone H4 hyperacetylation induced by sodium butyrate and the extent to which nucleosomes lose their compact shape and become elongated (62.0% of the particles have a length/width ratio over 1.6; overall mean in the length/width ratio = 1.83±0.48) when bound to electron microscope specimen grids at low ionic strength (1mM EDTA, 10mM Tris, pH 8.0). A marked proportion of elongated core particles is also observed in the naturally occurring hyperacetylated chicken testis chromatin undergoing spermatogenesls when analyzed at low Ionic strength (36.8% of the particles have a length/width ratio over 1.6). Core particles of elongated shape (length/width ratio over 1.6) generated under low ionic strength conditions are absent in the hypoacetylated chicken erythrocyte chromatin and represent only 2.3% of the untreated Hela S3 cell core particles containing a low proportion of hyperacetylated histones. The marked differences between control and hyperacetylated core particles are absent if the particles are bound to the carbon support film in the presence of 0.2 M NaCI, 6mM MgCI2 and 10mM Tris pH 8.0, conditions known to stabilize nucleosomes. A survey of the published work on histone hyperacetylation together with the present results indicate that histone hyperacetylation does not produce any marked disruption of the core particle per se’ yybut that it decreases intranucleosomal stabilizing forces as judged by the lowered stability of the hyperacetylated core particle under conditions of shearing stress such as cationic competition by the carbon support film of the EM grid for DNA binding.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  S. A. Georges, W. L. Kraus, K. Luger, J. K. Nyborg, and P. J. Laybourn p300-Mediated Tax Transactivation from Recombinant Chromatin: Histone Tail Deletion Mimics Coactivator Function Mol. Cell. Biol., January 1, 2002; 22(1): 127 - 137. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. P. Bazett-Jones, J. Cote, C. C. Landel, C. L. Peterson, and J. L. Workman The SWI/SNF Complex Creates Loop Domains in DNA and Polynucleosome Arrays and Can Disrupt DNA-Histone Contacts within These Domains Mol. Cell. Biol., February 1, 1999; 19(2): 1470 - 1478. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Ranganna and F. M. Yatsu Inhibition of Platelet-Derived Growth Factor BB–Induced Expression of Glyceraldehyde- 3-Phosphate Dehydrogenase by Sodium Butyrate in Rat Vascular Smooth Muscle Cells Arterioscler. Thromb. Vasc. Biol., December 1, 1997; 17(12): 3420 - 3427. [Abstract] [Full Text]
|
|
|
|
 |
|
 G. J. Czarnota and F. P. Ottensmeyer Structural States of the Nucleosome J. Biol. Chem., February 16, 1996; 271(7): 3677 - 3683. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Garcia-Ramirez, C. Rocchini, and J. Ausio Modulation of Chromatin Folding by Histone Acetylation J. Biol. Chem., July 28, 1995; 270(30): 17923 - 17928. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L A Stargell, J Bowen, C A Dadd, P C Dedon, M Davis, R G Cook, C D Allis, and M A Gorovsky Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila. Genes & Dev., December 1, 1993; 7(12b): 2641 - 2651. [Abstract] [PDF]
|
|
|
|
|
|
R Lin, R G Cook, and C D Allis Proteolytic removal of core histone amino termini and dephosphorylation of histone H1 correlate with the formation of condensed chromatin and transcriptional silencing during Tetrahymena macronuclear development. Genes & Dev., September 1, 1991; 5(9): 1601 - 1610. [Abstract] [PDF]
|
|