Nucleic Acids Research, Vol 25, Issue 18 3693-3697, Copyright © 1997 by Oxford University Press
DD Leipe and D Landsman
Searches of several sequence databases reveal that human HD1, yeast HDA1,
yeast RPD3 and other eukaryotic histone deacetylases share nine motifs with
archaeal and eubacterial enzymes, including acetoin utilization protein
(acuC) and acetylpolyamine amidohydrolase. Histone deacetylase and
acetylpolyamine amidohydrolase also share profound functional similarities
in that both: (i) recognize an acetylated aminoalkyl group; (ii) catalyze
the removal of the acetyl group by cleaving an amide bond; (iii) increase
the positive charge of the substrate. Stabilization of nucleosomal
DNA-histone interaction brought about by the change in charge has been
implicated as the underlying cause for histone deacetylase-mediated
transcriptional repression. We speculate that the eukaryotic histone
deacetylases originated from a prokaryotic enzyme similar to the
acetylpolyamine amidohydrolases that relied on reversible acetylation and
deacetylation of the aminoalkyl group of a DNA binding molecule to achieve
a gene regulatory effect.
ARTICLES
Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20984, USA.
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