Histone target selection within chromatin: an exemplary case of teamwork.
Histone modifiers like acetyltransferases, methyltransferases, and demethylases are critical regulators of most DNA-based nuclear processes, de facto controlling cell cycle progression and cell fate. These enzymes perform very precise post-translational modifications on specific histone residues, which in turn are recognized by different effector modules/proteins. We now have a better understanding of how these enzymes exhibit such specificity. As they often reside in multisubunit complexes, they use associated factors to target their substrates within chromatin structure and select specific histone mark-bearing nucleosomes. In this review, we cover the current understanding of how histone modifiers select their histone targets. We also explain how different experimental approaches can lead to conflicting results about the histone specificity and function of these enzymes.
St-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Centre de Recherche du CHU de Québec-Axe Oncologie, Hôtel-Dieu de Québec, Quebec City, Quebec G1R 2J6, Canada.
Marie-Eve
ME
Lalonde
St-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Centre de Recherche du CHU de Québec-Axe Oncologie, Hôtel-Dieu de Québec, Quebec City, Quebec G1R 2J6, Canada.
Xue
X
Cheng
St-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Centre de Recherche du CHU de Québec-Axe Oncologie, Hôtel-Dieu de Québec, Quebec City, Quebec G1R 2J6, Canada.
Jacques
J
Côté
D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D009707:Nucleosomes / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D022661:RNA, Untranslated / Q000378:metabolism; D013379:Substrate Specificity
D002843:Chromatin; D004798:Enzymes; D006657:Histones; D009707:Nucleosomes; D022661:RNA, Untranslated
acetyltransferases; chromatin readers; histone tails; histone-modifying complexes; methyltransferases