Inhibition of histone acetylation by N-[2-(S-coenzyme A)acetyl] spermidine amide, a multisubstrate analog
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 acetylatio...
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Veröffentlicht in: | The Journal of biological chemistry 1982-10, Vol.257 (20), p.12165-12169 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)33695-0 |