Journal
EMBO REPORTS
Volume 7, Issue 4, Pages 397-403Publisher
WILEY
DOI: 10.1038/sj.embor.7400625
Keywords
lysine methylation; protein-domain arrays; tudor domain
Categories
Funding
- NIDDK NIH HHS [R01 DK062248, R56 DK062248, DK62248] Funding Source: Medline
- NIEHS NIH HHS [ES011047, P30 ES007784, ES07784, U01 ES011047] Funding Source: Medline
- NIGMS NIH HHS [GM68804, R01 GM068804] Funding Source: Medline
Ask authors/readers for more resources
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-lysinebinding protein modules, and also demonstrates that proteindomain microarrays are powerful tools for the identification of new domain types that recognize histone modifications.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available