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Posttranslational modification of chromatin by histone methylation has wide-ranging effects on nuclear function, including transcriptional regulation, maintenance of genome integrity, and epigenetic inheritance. The enzymes utilized to place histone methylation marks are well characterized, but the identity of a histone demethylation system remained elusive until recently. The discovery of histone demethylase enzymes capable of directly removing methyl groups from modified lysine residues has demonstrated that histone methylation is a dynamic modification. The most extensive family of histone demethylase enzymes identified so far contains a JmjC domain and catalyzes demethylation through a hydroxylation reaction. Here, we identify PLU-1, a transcriptional repressor implicated in breast cancer, as a histone demethylase enzyme that has the ability to reverse the trimethyl H3K4 modification state. Furthermore, we reveal that PLU-1-mediated H3K4 demethylase activity plays an important role in the proliferative capacity of breast cancer cells through repression of tumor suppressor genes, including BRCA1.

Original publication




Journal article


Mol Cell

Publication Date





801 - 812


Amino Acid Sequence, Breast Neoplasms, Cell Cycle, Cell Division, Cell Line, Tumor, DNA-Binding Proteins, Female, Gene Expression Regulation, Neoplastic, Humans, Jumonji Domain-Containing Histone Demethylases, Molecular Sequence Data, Nuclear Proteins, Repressor Proteins, Transcription, Genetic