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Two classes of histone acetylation in developing mouse mammary gland.

W. Marzluff,K. McCarty

Published 1970 in Journal of Biological Chemistry

ABSTRACT

Abstract Mouse mammary gland explants rapidly incorporated 14C-acetate into the F1, F2a1, F2a2, and F3 histones. These acetylated histones were divided into two classes which were distinguished by their metabolic stability, electrophoretic mobility, and sensitivity to cycloheximide. The acetylation of the F1 and F2a2 histones was inhibited by cycloheximide, occurred only during their synthesis, and was limited to the α-amino group of the terminal serine. In contrast, the preformed F3 and F2a1 were acetylated on the e-NH2 group of internal lysine residues. This acetate was unstable, and the histones were rapidly deacetylated. The F2b histone did not incorporate 14C-acetate. These results suggest that amino-terminal acetylation of the F1, F2a1, and F2a2 histones represents a mechanism of polypeptide chain initiation in eucaryotic cells analogous to aminoterminal formylation in procaryotic cells. If acetylation of histones has a functional role by modifying the DNA-histone interaction, it is reasonable to assume that this modification must also be reversible. Since the acetylation of both F1 and F2a2 histones occurs only during their synthesis, and this acetate remains with the stable histone, it is unlikely that these proteins function in a reversible DNA association. In contrast, both the F2a1 and F3 histone fractions are reversibly acetylated on preformed molecules, suggesting that acetylation of these proteins could function in the control of RNA transcription.

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