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Sendra R, Rodrigo I, Salvador ML, et al. Characterization of pea histone deacetylases. Plant Mol Biol. 1988;11(6):857-66doi: 10.1007/BF00019525.
Sendra, R., Rodrigo, I., Salvador, M. L., & Franco, L. (1988). Characterization of pea histone deacetylases. Plant molecular biology, 11(6), 857-66. https://doi.org/10.1007/BF00019525
Sendra, R, et al. "Characterization of pea histone deacetylases." Plant molecular biology vol. 11,6 (1988): 857-66. doi: https://doi.org/10.1007/BF00019525
Sendra R, Rodrigo I, Salvador ML, Franco L. Characterization of pea histone deacetylases. Plant Mol Biol. 1988 Nov;11(6):857-66. doi: 10.1007/BF00019525. PMID: 24272635.
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Plant Mol Biol. 1988 Nov;11(6):857-66. doi: 10.1007/BF00019525.

Characterization of pea histone deacetylases.

Plant molecular biology

R Sendra, I Rodrigo, M L Salvador, L Franco

Affiliations

  1. Department of Biochemistry and Molecular Biology, Faculties of Sciences, University of Valencia, Burjassot, 46100, Valencia, Spain.

PMID: 24272635 DOI: 10.1007/BF00019525

Abstract

The present paper is the first report on histone deacetylases from plants. Three enzyme fractions with histone deacetylase activity (HD0, HD1 and HD2) have been partially purified from pea (Pisum sativum) embryonic axes. They deacetylate biologically acetylated chicken histones and, to a lesser extent, chemically acetylated histones, this being a criterion of their true histone deacetylase nature. The three enzymes are able to accept nucleosomes as substrates. HD1 is not inhibited by n-butyrate up to 50 mM, whereas HD0 and HD2 are only slightly inhibited, thereby establishing a clear difference to animal histone deacetylases. The three activities are inhibited by acetate, Cu(2+) and Zn(2+) ions and mercurials, but are only scarcely affected by polyamines, in strong contrast with yeast histone deacetylase. Several criteria have been used to obtain cumulative evidence that HD0, HD1 and HD2 actually are three distinct enzymes. In vitro experiments with free histones show that HD0 deacetylates all four core histones, whereas HD1 and HD2 show a clear preference for H2A and H2B, the arginine-rich histones being deacetylated more slowly.

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