Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Histone H3K4 Demethylation is Negatively Regulated by Histone H3 Acetylation in S. cerevisiae


ABSTRACT: Histone H3 lysine 4 tri-methylation (H3K4me3) is a hallmark of transcription initiation, but how H3K4me3 is demethylated during gene repression is poorly understood. Jhd2, a JmjC domain protein, was recently identified as the major H3K4me3 histone demethylase (HDM) in S. cerevisiae. While JHD2 is required for removal of methylation upon gene repression, deletion of JHD2 does not result in increased levels of H3K4me3 in bulk histones, indicating that this HDM is unable to demethylate histones during steady state conditions. In this study, we showed that this was due to the negative regulation of Jhd2 activity by histone H3 lysine 14 acetylation, which co-localizes with H3K4me3 across the yeast genome. We demonstrated that loss of the histone H3-specific acetyltransferases (HATs) resulte

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Benjamin Martin 

PROVIDER: E-GEOD-41424 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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