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Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27 and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound...

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Detalhes bibliográficos
Main Authors: Tang, Yong, Holbert, Marc A., Delgoshaie, Neda, Wurtele, Hugo, Guillemette, Benoît, Meeth, Katrina, Yuan, Hua, Drogaris, Paul, Lee, Eun-Hye, Durette, Chantal, Thibault, Pierre, Verreault, Alain, Cole, Philip A., Marmorstein, Ronen
Formato: Artigo
Idioma:Inglês
Publicado em: 2011
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3050538/
https://ncbi.nlm.nih.gov/pubmed/21256037
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2010.12.012
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