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J Biol Chem, Vol. 275, Issue 17, 13007-13011, April 28, 2000
From the Division of Cell Biology and Biophysics, School of
Biological Sciences, University of Missouri, Kansas City Missouri
64110-2499
The importance of control of the levels of
histone acetylation for the control of gene expression in eukaryotic
chromatin is being elucidated, and the yeast Saccharomyces
cerevisiae has proven to be an important model system. The level
of histone acetylation in yeast is the highest known. However, only
acetylation of H4 has been quantified, and reports reveal loss of
acetylation in histone preparations. A chaotropic guanidine-based
method for histone isolation from intact wild-type cells or from a
single-step nuclear preparation with butyrate preserves acetylation of
all core histones. Histone H4 has an average of more than 2 acetylated lysines per molecule, distributed over 4 sites. Histones H2A, H3, and
H2B have 0.2, ~2, and >2 acetylated lysines per molecule, respectively, distributed across 2, 5, and 6 sites. Thus, yeast nucleosomes carry, on average, 13 acetylated lysines per octamer, i.e. just above the threshold of 10
Steady-state Levels of Histone Acetylation in Saccharomyces
cerevisiae*
12 deduced for
transcriptionally activated chromatin of animals, plants, and algae.
Following Mr 100,000 ultrafiltration in 2.5%
acetic acid, yeast histone H3 was purified to homogeneity by
reversed-phase high pressure liquid chromatography. Other core histones
were obtained at 8095% purity.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Rm. 414 BSB, 5007 Rockhill Rd., Kansas City, MO 64110-2499. Tel.: 816-235-2591; Fax:
816-235-5158; E-mail: WaterborgJ@umkc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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