The Histone Demethylases JMJD1A and JMJD2B Are Transcriptional Targets of Hypoxia-inducible Factor HIF

• Published in: The Journal of biological chemistry Vol. 283; no. 52; pp. 36542 - 36552
• Main Authors: Beyer, Sophie, Kristensen, Malene Maag, Jensen, Kim Steen, Johansen, Jens Vilstrup, Staller, Peter
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.12.2008; American Society for Biochemistry and Molecular Biology
• Subjects: Arginine - chemistry; Base Sequence; Gene Expression Regulation; HeLa Cells; Histone Deacetylases - metabolism; Histones - chemistry; Humans; Hypoxia; Hypoxia-Inducible Factor 1 - metabolism; Jumonji Domain-Containing Histone Demethylases; Kidney - embryology; Lysine - chemistry; Microscopy, Fluorescence; Molecular Sequence Data; Oxidoreductases, N-Demethylating - physiology; Transcription Factors - physiology; Transcription, Chromatin, and Epigenetics

Posttranslational histone modifications serve to store epigenetic information and control both nucleosome assembly and recruitment of non-histone proteins. Histone methylation occurs on arginine and lysine residues and is involved in the regulation of gene transcription. A dynamic control of these m...