Snf1 - a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription

Modification of histories is an important element in the regulation of gene expression. Previous work suggested a link between acetylation and phospho rylation, but questioned its mechanistic basis. We have purified a histone H3 serine-10 kinase complex from Saccharomyces cerevisiae and have identifi ed its catalytic subunit as Snf1. The Snf1/AMPK family of kinases function in conserved signal transduction pathways. Our results show that Snf1 and t he acetyltransferase Gcn5 function in an obligate sequence to enhance INO1 transcription by modifying histone H3 serine-10 and lysine-14. Thus, phosph orylation and acetylation are targeted to the same histone by promoter-spec ific regulation by a kinase/acetyltransferase pair, supporting models of ge ne regulation wherein transcription is controlled by coordinated patterns o f histone modification.