Histone acetylation during meiosis in Lilium microsporocytes

Abstract

Acetate incorporation into histones of Lilium microsporocytes is consistently higher in early prophase of meiosis than in later stages. The pattern of acetate incorporation into histones differs from that found for the soluble nuclear proteins. Evidence is presented that acetate incorporation reflects true acetylation, not histone synthesis. e- N-acetyllysine (eNAcLys) was released from histones by enzymatic digestion. Amino acid analysis of the digests confirm the presence of significantly higher amounts of eNAcLys in early meiotic stages. These results are consistent with the hypothesis that modulation of histone charge plays a role in the binding of histones to DNA and/or chromosome condensation. In vitro levels of histone acetylating activity remain constant throughout meiosis. The results suggest that microsporocyte histone deacetylase activity increases through meiotic prophase.