histone modifications

This article was first published by EpigenTek. In the early 1960s, Vincent G. Allfrey and his colleagues at the Rockefeller Institute (today’s Rockefeller University) demonstrated by way of C14 labeling the incorporation of methyl and acetyl groups into histones.1 The evidence suggested that these chemical additions succeeded protein synthesis, although the means by which they were incorporated as well as the extent of their biological significance were not fully understood at the time. Allfrey’s pioneering work effectively laid the foundation for histone [more…]

Recently Dr. Yu Xue’s group, at the Huazhong University of Science and Technology in Wuhan, China, developed a database designated as Eukaryotic Writers, Erasers and Readers protein of Histone Acetylation and Methylation system Database (WERAM). WERAM is a comprehensive database containing integrated information on the writers, erasers, and readers of histone acetylation and methylation. Namely writers are the enzymes that catalyze acetylation and methylation, the erasers are the enzymes that remove these marks, and the readers are proteins that recognize and interact [more…]

Post-translational modifications are well known for their influence on protein stability, enzymatic functions, as well as protein:protein interactions. At the level of gene expression, acetylation, methylation, phosphorylation, ADP-ribosylation, ubiquitination and SUMOylation are some of the most prevalent chemical modifications that regulate transcription factors and the chromatin template (the complex of DNA and histone proteins) alike. In particular, the manifold modifications occurring on the histone proteins that closely associate with DNA are proposed to constitute a gene-regulating code (the histone code). [more…]