Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 2009 Jan;1789(1):45-57
Date
07/08/2008Pubmed ID
18603028Pubmed Central ID
PMC2642981DOI
10.1016/j.bbagrm.2008.06.005Scopus ID
2-s2.0-59349115177 (requires institutional sign-in at Scopus site) 300 CitationsAbstract
Histone lysine and arginine residues are subject to a wide array of post-translational modifications including methylation, citrullination, acetylation, ubiquitination, and sumoylation. The combinatorial action of these modifications regulates critical DNA processes including replication, repair, and transcription. In addition, enzymes that modify histone lysine and arginine residues have been correlated with a variety of human diseases including arthritis, cancer, heart disease, diabetes, and neurodegenerative disorders. Thus, it is important to fully understand the detailed kinetic and chemical mechanisms of these enzymes. Here, we review recent progress towards determining the mechanisms of histone lysine and arginine modifying enzymes. In particular, the mechanisms of S-adenosyl-methionine (AdoMet) dependent methyltransferases, FAD-dependent demethylases, iron dependent demethylases, acetyl-CoA dependent acetyltransferases, zinc dependent deacetylases, NAD(+) dependent deacetylases, and protein arginine deiminases are covered. Particular attention is paid to the conserved active-site residues necessary for catalysis and the individual chemical steps along the catalytic pathway. When appropriate, areas requiring further work are discussed.
Author List
Smith BC, Denu JMAuthor
Brian C. Smith PhD Associate Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsArginine
Catalysis
Catalytic Domain
DNA
Histones
Humans
Lysine
Protein Processing, Post-Translational
