Literature DB >> 3301411

Polyamines inhibit the yeast histone deacetylase.

Q A Vu, D E Zhang, Z C Chroneos, D A Nelson.   

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.

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Year:  1987        PMID: 3301411     DOI: 10.1016/0014-5793(87)80879-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Characterization of pea histone deacetylases.

Authors:  R Sendra; I Rodrigo; M L Salvador; L Franco
Journal:  Plant Mol Biol       Date:  1988-11       Impact factor: 4.076

2.  Alkyl-substituted polyaminohydroxamic acids: a novel class of targeted histone deacetylase inhibitors.

Authors:  Sheeba Varghese; Deepak Gupta; Tiffany Baran; Anchalee Jiemjit; Steven D Gore; Robert A Casero; Patrick M Woster
Journal:  J Med Chem       Date:  2005-10-06       Impact factor: 7.446

3.  Selective use of H4 acetylation sites in the yeast Saccharomyces cerevisiae.

Authors:  D J Clarke; L P O'Neill; B M Turner
Journal:  Biochem J       Date:  1993-09-01       Impact factor: 3.857

4.  Properties of the yeast nuclear histone deacetylase.

Authors:  M M Sanchez del Pino; G Lopez-Rodas; R Sendra; V Tordera
Journal:  Biochem J       Date:  1994-11-01       Impact factor: 3.857

  4 in total

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