The S. 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 S. 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 sequences are cr

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Gregory Hogan 

PROVIDER: E-GEOD-7627 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress