Polyamines inhibit the yeast histone deacetylase

Quang A. Vu; Dong er Zhang; Zissis C. Chroneos; Daniel A. Nelson

doi:10.1016/0014-5793(87)80879-7

Polyamines inhibit the yeast histone deacetylase

Quang A. Vu, Dong er Zhang, Zissis C. Chroneos, Daniel A. Nelson

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	79-83
Number of pages	5
Journal	FEBS Letters
Volume	220
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(87)80879-7
State	Published - Aug 10 1987

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(87)80879-7

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title = "Polyamines inhibit the yeast histone deacetylase",

abstract = "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.",

author = "Vu, {Quang A.} and Zhang, {Dong er} and Chroneos, {Zissis C.} and Nelson, {Daniel A.}",

note = "Funding Information: This research was supported by a Limited-Grant-in-Aid from the University of Houston, and by a Biomedical Research Support Grant.",

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T1 - Polyamines inhibit the yeast histone deacetylase

AU - Vu, Quang A.

AU - Zhang, Dong er

AU - Chroneos, Zissis C.

AU - Nelson, Daniel A.

N1 - Funding Information: This research was supported by a Limited-Grant-in-Aid from the University of Houston, and by a Biomedical Research Support Grant.

PY - 1987/8/10

Y1 - 1987/8/10

N2 - 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.

AB - 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.

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Polyamines inhibit the yeast histone deacetylase

Abstract

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