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Chromatin methylation activity of Dnmt3a and Dnmt3a/3L is guided by interaction of the ADD domain with the histone H3 tail

Using peptide arrays and binding to native histone proteins, we show that the ADD domain of Dnmt3a specifically interacts with the H3 histone 1–19 tail. Binding is disrupted by di- and trimethylation of K4, phosphorylation of T3, S10 or T11 and acetylation of K4. We did not observe binding to the H4...

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Hlavní autoři: Zhang, Yingying, Jurkowska, Renata, Soeroes, Szabolcs, Rajavelu, Arumugam, Dhayalan, Arunkumar, Bock, Ina, Rathert, Philipp, Brandt, Ole, Reinhardt, Richard, Fischle, Wolfgang, Jeltsch, Albert
Médium: Artigo
Jazyk:Inglês
Vydáno: Oxford University Press 2010
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2910041/
https://ncbi.nlm.nih.gov/pubmed/20223770
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkq147
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