| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979177 | Current Opinion in Structural Biology | 2011 | 6 Pages |
Eukaryotic DNA is packaged into chromatin, a complex assembly of protein and nucleic acid. The histones within chromatin undergo extensive, highly regulated post-translational modification. One of the main functions of these modifications is to act as markers that ensure that the mutiprotein complexes that regulate the transcription, replication and repair of DNA are directed to the correct region of the genome at the appropriate time. This review focuses on recent biochemical and structural studies on how histones modified by acetylation, ubiquitination, phosphorylation and poly-ADP-ribosylation are recognized.
► A single bromodomain can bind two acetylation marks on a histone tail. ► Acetylated lysine residues in histones can be recognized by PHD fingers. ► PHD finger bromodomains cassettes can interpret modification patterns on a single histone or on two histones within a nucleosome. ► The BIR domain of Survivin binds to histone H3 phosphorylated on threonine 3. ► PolyADP-ribosylated and polyubiquitinated histones can be recognized by modification specific domains.
