The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2.

ABSTRACT: Histone methylation plays important roles in the regulation of chromatin dynamics and transcription. Steady-state levels of histone lysine methylation are regulated by a balance between enzymes that catalyze either the addition or removal of methyl groups. Using an activity-based biochemical approach, we recently uncovered the JmjC domain as an evolutionarily conserved signature motif for histone demethylases. Furthermore, we demonstrated that Jhd1, a JmjC domain-containing protein in Saccharomyces cerevisiae, is an H3K36-specific demethylase. Here we report further characterization of Jhd1. Similar to its mammalian homolog, Jhd1-catalyzed histone demethylation requires iron and alpha-ketoglutarate as cofactors. Mutation and deletion studies indicate that the JmjC domain and adjacent seque

SUBMITTER: Fang J 

PROVIDER: S-EPMC1951470 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature