Polyamines inhibit the yeast histone deacetylase

n-Butyrate inhibits the histone deacetylase from higher cells, but has little effect on the enzyme activity in Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The util...

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Veröffentlicht in:FEBS letters 1987-08, Vol.220 (1), p.79-83
Hauptverfasser: Vu, Quang A., Zhang, Dong-er, Chroneos, Zissis C., Nelson, Daniel A.
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container_title FEBS letters
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creator Vu, Quang A.
Zhang, Dong-er
Chroneos, Zissis C.
Nelson, Daniel A.
description n-Butyrate inhibits the histone deacetylase from higher cells, but has little effect on the enzyme activity in Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The utility of these inhibitors was demonstrated by showing that 2 mM spermine substantially increased the incorporation of [ 3H]acetate into histone in a yeast nuclear acetyltransferase assay.
doi_str_mv 10.1016/0014-5793(87)80879-7
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subjects Acetates - metabolism
Amidohydrolases - antagonists & inhibitors
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Histone deacetylase
Histone Deacetylase Inhibitors
Hydrolases
Mes, 4-morpholineethanesulfonic acid
n-Butyrate
PMSF, phenylmethylsulfonyl fluoride
Polyamines - pharmacology
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Spermidine
Spermidine - pharmacology
Spermine
Spermine - pharmacology
title Polyamines inhibit the yeast histone deacetylase
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