Histone glutamine methylation afFACTing rDNA transcription

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2014,（3）
• 页码范围: 261-262
• 页数: 2页
• 语种: 英文
• DOI: 10.1038/cr.2014.22

摘要

Chemical modifications of histone proteins directly and indirectly affect chromatin structure and thereby contribute to the multilayered control of diverse DNA-based processes.A recent study in Nature enriches this list of enzyme-dependent posttransiational histone marks by H2A glutamine methylation that appears to be dedicated to only one specific cellular process,the regulation of nucleolar rDNA transcription. Decades of research have highlighted the importance ofposttranslational protein modifications as means to regulate diverse cellular processes,such as signal transduction pathways,metabolic functions and gene expression.Histones,the proteinaceous constituents of the packaged eukaryotic genetic information called chromatin,are decorated with a vast amount of diverse posttranslational modifications (PTMs) that differ in their chemical nature,residue location and,ultimately,their biochemical effects on DNA-based processes [1].Lysine acetylation,lysine and arginine methylation,as well as serine and threonine phosphorylation are so far the best studied histone marks among many others and help to locally manipulate DNA accessibility of the chromatin structure to control gene regulation,DNA repair,mitosis and apoptosis.