6533b832fe1ef96bd129ae99

RESEARCH PRODUCT

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

Georg GoldererGerardo López-rodasGerardo López-rodasPeter LoidlHerbert LindnerGerald BroschPeter Gröbner

subject

ErythrocytesSaccharomyces cerevisiae ProteinsBiophysicsBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesPhysarumHistone H1AcetyltransferasesPhysarum polycephalumStructural BiologyHistone H2AGeneticsAnimalsHistone deacetylaseHistone octamerMolecular BiologyChromatography High Pressure LiquidHistone AcetyltransferasesHistone AcetyltransferasesbiologyHistone deacetylase 2AcetylationButyrateCell BiologyHistone acetyltransferaseMolecular biologyChromatinHistone Deacetylase InhibitorsIsoenzymesButyratesKineticsHistone acetylationBiochemistryHistone methyltransferasebiology.proteinButyric AcidHistone acetyltransferaseHistone deacetylaseChickensProtein Processing Post-Translational

description

DEAE-Scpharose chromatography of extracts from plasmodia of the myxomyccte PI~.~suru~~t ,~/.~crpl~~ho~~ revealed the presence of multiple histone acetyltransferases and histonc deacctylascs. A cyloplasmic histonc acctyltransferase B, specific for histonc H4, and two nuclear acetyltransferases Al and A2 were identilied; Al acetylates all core hislones with a preference for l-13 and H2A. whereas A2 is specific for H3 and also slightly for H2B. Two hislone deacetylases. HDI and HD2, could be discriminated. They differ with respect to subslralc speciliciiy and pH dependence. For the first time the substrate specificity of histonc deacetylascs was determined using HPLC-purilicd individual core histonc spccics. The order of acetylated substrate preference is H?A;~H~zH~>H~B for HDI and H3sH2ArH4 for HD2, respectively; HD2 is inactive with I-f213 BS substralc. Moreover histone deacetylases arc very sensitive to butyrate. since 2 mM butyrate leads to more than 50% inhibition of enzyme activity. Histonc acctylation; Histone acctyltronsferase; Histone dcacetylase; Butyrate; Chromalin; PI~~‘surl~/n

yearjournalcountryeditionlanguage
1992-01-13FEBS Letters
https://doi.org/10.1016/0014-5793(92)80408-9