期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 27, 期 13, 页码 5055-5065出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.00127-07
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资金
- NIGMS NIH HHS [R01 GM068804, GM072518, R01 GM072518-03, GM68804, R01 GM072518, R01 GM072518-01A1, R01 GM072518-02] Funding Source: Medline
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 Jhdl, a JmjC domain-containing protein in Saccharomyces cerevisiae, is an H3K36-specific demethylase. Here we report further characterization of Jhdl. Similar to its mammalian homolog, Jhd1-catalyzed histone demethylation requires iron and a-ketoglutarate as cofactors. Mutation and deletion studies indicate that the JmjC domain and adjacent sequences are critical for Jhdl enzymatic activity, while the N-terminal PHD domain is dispensable. Overexpression of JHD1 results in a global reduction of H3K36 methylation in vivo. Finally, chromatin immunoprecipitation-coupled microarray studies reveal subtle changes in the distribution of H3K36me2 upon overexpression or deletion of JHD1. Our studies establish Jhdl as a histone demethylase in budding yeast and suggest that Jhdl functions to maintain the fidelity of histone methylation patterns along transcription units.
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