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Many of the enzymes that lay down this code have been identified. However, so far, few code\u2010reading proteins have been identified. Here, we describe a protein\u2010array approach for identifying methyl\u2010specific interacting proteins. We found that not only chromo domains but also tudor and MBT domains bind to methylated peptides from the amino\u2010terminal tails of histones H3 and H4. Binding specificity observed on the protein\u2010domain microarray was corroborated using peptide pull\u2010downs, surface plasma resonance and far western blotting. Thus, our studies expose tudor and MBT domains as new classes of methyl\u2010lysine\u2010binding protein modules, and also demonstrates that protein\u2010domain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.<\/jats:p>","DOI":"10.1038\/sj.embor.7400625","type":"journal-article","created":{"date-parts":[[2006,1,13]],"date-time":"2006-01-13T08:12:47Z","timestamp":1137139967000},"page":"397-403","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":408,"title":["Tudor, MBT and chromo domains gauge the degree of lysine methylation"],"prefix":"10.1038","volume":"7","author":[{"given":"Jeesun","family":"Kim","sequence":"first","affiliation":[{"name":"The University of Texas M.D. Anderson Cancer Center, Science Park\u2010Research Division  PO Box 389 Smithville Texas 78957 USA"}]},{"given":"Jeremy","family":"Daniel","sequence":"additional","affiliation":[{"name":"The 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