title: For a healthy histone code, a little SUMO in the tail keeps the acetyl away.
abstract: Chemical modification of histones through a growing number of post-translational mechanisms is an integral part of transcription. A recent report provides exciting new evidence that conjugation of the ubiquitin-like protein SUMO to histones opposes acetylation and establishes SUMOylation as an important histone mark linked to transcriptional repression.
authors.affiliation: Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0632, USA. iniguez@umich.edu
authors.forename: Jorge A
authors.initials: JA
authors.lastname: Iñiguez-Lluhí
mesh_terms: D000107:Acetylation; D000818:Animals; D042421:Histone Code / Q000502:physiology*; D006801:Humans; D025841:Small Ubiquitin-Related Modifier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D025841:Small Ubiquitin-Related Modifier Proteins