{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim J"],"funding":["NIDDK NIH HHS","NIEHS NIH HHS","NIGMS NIH HHS"],"pagination":["397-403"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1456902"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(4)"],"pubmed_abstract":["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."],"journal":["EMBO reports"],"pubmed_title":["Tudor, MBT and chromo domains gauge the degree of lysine methylation."],"pmcid":["PMC1456902"],"funding_grant_id":["ES07784","DK62248","GM68804","R56 DK062248","ES011047","U01 ES011047","R01 GM068804","P30 ES007784","R01 DK062248"],"pubmed_authors":["Daniel J","Espejo A","Xia L","Bedford MT","Zhang Y","Lake A","Kim J","Krishna M"],"additional_accession":[]},"is_claimable":false,"name":"Tudor, MBT and chromo domains gauge the degree of lysine methylation.","description":"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.","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Apr","modification":"2026-03-16T16:10:41.659Z","creation":"2019-03-27T01:26:23Z"},"accession":"S-EPMC1456902","cross_references":{"pubmed":["16415788"],"doi":["10.1038/sj.embor.7400625"]}}