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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Detalles Bibliográficos
Autores principales: Zhang, Yingying, Jurkowska, Renata, Soeroes, Szabolcs, Rajavelu, Arumugam, Dhayalan, Arunkumar, Bock, Ina, Rathert, Philipp, Brandt, Ole, Reinhardt, Richard, Fischle, Wolfgang, Jeltsch, Albert
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Gene Regulation, Chromatin and Epigenetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2910041/
https://www.ncbi.nlm.nih.gov/pubmed/20223770
http://dx.doi.org/10.1093/nar/gkq147

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