Premium
Tudor, MBT and chromo domains gauge the degree of lysine methylation
Author(s) -
Kim Jeesun,
Daniel Jeremy,
Espejo Alexsandra,
Lake Aimee,
Krishna Murli,
Xia Li,
Zhang Yi,
Bedford Mark T
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400625
Subject(s) - histone , bromodomain , biology , computational biology , histone code , histone h3 , histone methyltransferase , lysine , microbiology and biotechnology , genetics , dna , amino acid , nucleosome
The post‐translational modification of histones regulates many cellular processes, including transcription, replication and DNA repair. A large number of combinations of post‐translational modifications are possible. This cipher is referred to as the histone code. Many of the enzymes that lay down this code have been identified. However, so far, few code‐reading proteins have been identified. Here, we describe a protein‐array approach for identifying methyl‐specific interacting proteins. We found that not only chromo domains but also tudor and MBT domains bind to methylated peptides from the amino‐terminal tails of histones H3 and H4. Binding specificity observed on the protein‐domain microarray was corroborated using peptide pull‐downs, surface plasma resonance and far western blotting. Thus, our studies expose tudor and MBT domains as new classes of methyl‐lysine‐binding protein modules, and also demonstrates that protein‐domain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.