Physicochemical modifications of histones and their impact on epigenomics.
The study of histone post-translational modifications (PTMs) has made extraordinary progress over the past few years and many epigenetic modifications have been identified and found to be associated with fundamental biological processes and pathological conditions. Most histone-modifying enzymes produce specific covalent modifications on histone tails that, taken together, elicit complex and concerted processes. An even higher level of complexity is generated by the action of small molecules that are able to modulate pharmacologically epigenetic enzymes and interfere with these biochemical mechanisms. In this article, we provide an overview of histone PTMs by reviewing and discussing them in terms of their physicochemical properties, emphasizing these concepts in view of recent research efforts to elucidate epigenetic mechanisms and devise future epigenetic drugs.
Department of Experimental, Diagnostic and Specialty Medicine (DIMES), Alma Mater Studiorum, University of Bologna, Via S. Giacomo 14, Bologna 40126, Italy.
Federico
F
Andreoli
Department of Experimental, Diagnostic and Specialty Medicine (DIMES), Alma Mater Studiorum, University of Bologna, Via S. Giacomo 14, Bologna 40126, Italy; Institute of Organic Synthesis and Photoreactivity, National Research Council, Via P. Gobetti, 101, Bologna 40129, Italy. Electronic address: alberto.delrio@gmail.com.
Alberto
A
Del Rio
D015195:Drug Design; D044127:Epigenesis, Genetic; D057890:Epigenomics; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational
D006657:Histones