A multisubstrate analog, formed by joining coenzyme A with spermidine through an acetic acid linkage, serves as a strong inhibitor (Ki less than 10(-8) M) of the acetylation of spermidine and histones by histone acetylase purified from calf thymus. In free solutions, this analog inhibited acetylation of the various nuclear histones to a similar extent. In isolated nuclei, this analog was found to inhibit acetylation of histones H2a and H2b very much more strongly than that of histones H3 and H4.
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Cullis et al. (1982) studied this question.
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