2L7P
ASHH2 a CW domain
Summary for 2L7P
| Entry DOI | 10.2210/pdb2l7p/pdb |
| NMR Information | BMRB: 17365 |
| Descriptor | Histone-lysine N-methyltransferase ASHH2, ZINC ION (2 entities in total) |
| Functional Keywords | cw-domain, transferase |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Nucleus (Probable): Q2LAE1 |
| Total number of polymer chains | 1 |
| Total formula weight | 11278.63 |
| Authors | Kristiansen, P.,Hoppmann, V.,Thorstensen, T.,Aalen, R.B.,Aasland, R.,Finne, K.,Veiseth, S. (deposition date: 2010-12-16, release date: 2011-05-11, Last modification date: 2024-05-01) |
| Primary citation | Hoppmann, V.,Thorstensen, T.,Kristiansen, P.E.,Veiseth, S.V.,Rahman, M.A.,Finne, K.,Aalen, R.B.,Aasland, R. The CW domain, a new histone recognition module in chromatin proteins. Embo J., 30:1939-1952, 2011 Cited by PubMed Abstract: Post-translational modifications of the N-terminal histone tails, including lysine methylation, have key roles in regulation of chromatin and gene expression. A number of protein modules have been identified that recognize differentially modified histone tails and provide their proteins with the capacity to sense such modifications. Here, we identify the CW domain of plant and animal chromatin-related proteins as a novel module that recognizes different methylated states of lysine 4 on histone H3 (H3K4me). The solution structure of the CW domain of the Arabidopsis ASH1 HOMOLOG2 (ASHH2) histone methyltransferase provides insight into how different CW domains can distinguish different methylated histone tails. We provide evidence that ASHH2 is acting on H3K4me-marked genes, allowing for ASHH2-dependent H3K36 tri-methylation, which contributes to sustained expression of tissue-specific and developmentally regulated genes. This suggests that ASHH2 is a combined 'reader' and 'writer' of the histone code. We propose that different CW domains, dependent on their specificity for different H3K4 methylations, are important for epigenetic memory or participate in switching between permissive and repressive chromatin states. PubMed: 21522130DOI: 10.1038/emboj.2011.108 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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