Abstract

A histone deacetylase activity has been found in preparation of chromatin from pea ( Pisum sativum) embryonic axes. This activity readily deacetylates free histones and is somewhat specific for H2A and H2B; this property and its chromatographic behaviour allowed us to identify the enzyme with the previously described histone deacetylase HD2 (Sendra et al., Plant Mol. Biol., 11 (1988) 857). HD2 is only loosely associated to chromatin but the enzymatic activity is enhanced when chromatin adopts a folded conformation. Polyamines and divalent cations activate the enzyme, probably due to their effect on chromatin folding.

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