Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum

FEBS Letters

Golderer, Georg¹  Gröbner, Peter¹  Brosch, Gerald²  Lindner, Herbert¹  Loidl, Peter²  López-Rodas, Gerardo² 

[1] Department of Medical Chemistry and Biochemistry, University of Innsbruck-Medical School, A-6020 Innsbruck, Austria;Department of Microbiology University of Innsbruck-Medical School, A-6020 Innsbruck, Austria

关键词: Histone acetylation;    Histone acetyltransferase;    Histone deacetylase;    Butyrate;    Chromatin;    Physarum;   

DOI  :  10.1016/0014-5793(92)80408-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

DEAE-Sepharose chromatography of extracts from plasmodia of the myxomycete Physarum polycephalum revealed the presence of multiple histone acetyltransferases and histone deacetylases. A cytoplasmic histone acetyltransferase B, specific for histone H4, and two nuclear acetyltransferases A1 and A2 were identified; A1 acetylates all core histones with a preference for H3 and H2A, whereas A2 is specific for H3 and also slightly for H2B. Two histone deacetylases, HD1 and HD2, could be discriminated. They differ with respect to substrate specificity and pH dependence. For the first time the substrate specificity of histone deacetylases was determined using HPLC-purified individual core histone species. The order of acetylated substrate preference is H2A>H3>-H4>H2B for HD1 and H3>H2A>H4 for HD2, respectively; HD2 is inactive with H2B as substrate. Moreover histone deacetylases are very sensitive to butyrate, since 2 mM butyrate leads to more than 50% inhibition of enzyme activity.

【 授权许可】

Unknown