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Regulation of histone acetyl transferase activity during the development of artemia salina


, : Regulation of histone acetyl transferase activity during the development of artemia salina. Developmental Biology 54(2): 276-287

Histone acetyltransferase activity was studied in 1 M KCl extracts from nuclear preparations of A. salina. The requirements for optimal activity included a slightly alkaline pH and the absence of mono- and divalent cations. Marked differences in histone saturation kinetics were observed in crude extract from early and late developmental stages. The sigmoidal-type curve observed in nauplii arose from the presence in these crude extracts of an inhibitor of acetyltransferase activity. Serial substrate-saturation studies with crude acetyltransferase preparations indicated accumulation of inhibitor at times of development, associated with a rapid increase in histone acetyltransferase activity. On the basis of its susceptibility to enzymatic hydrolysis and its gel-filtration behavior, the inhibitor was characterized as a small DNA sequence. Comparative studies of the Artemia inhibitor and sonicated calf thymus DNA indicated that in both cases the inhibition proceeded through a histone-DNA interaction that rendered the histone inaccessible to the acetyltransferase. These studies revealed marked differences in reversibility by protamines and in specificity for histone fractions between the inhibitor from Artemia and DNA from other sources.

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Related references

Cano, A.; Estepa, I.; Pestana, A., 1980: Substrate regulation of histone acetyl transferase ec 2.3.1.48 from artemia salina. Histone H1 is the best substrate for the histone acetyltransferase from A. salina, while the acetylation of unfractionated histones by the isolated enzyme or the acetylation of endogenous histones in nuclear suspensions is exclusively confined to...

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