Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-4-4
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-10445843, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-11242053, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-11242054, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-11389857, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-11498575, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12130538, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12137563, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12438239, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12575993, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12588862, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12800201, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12897052, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-12897054, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-14527417, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15123827, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15138608, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15145825, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15182349, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15520406, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15525939, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15550243, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15573092, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15647753, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15927959, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-15960974, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-16024779, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-3522591, http://linkedlifedata.com/resource/pubmed/commentcorrection/16415788-9581497
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1469-221X
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
397-403
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Tudor, MBT and chromo domains gauge the degree of lysine methylation.
pubmed:affiliation
The University of Texas MD Anderson Cancer Center, Science Park-Research Division, Smithville, 78957, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural