Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response

The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of hi...

Descripción completa

Detalles Bibliográficos
Autores principales: Shanle, Erin K., Andrews, Forest H., Meriesh, Hashem, McDaniel, Stephen L., Dronamraju, Raghuvar, DiFiore, Julia V., Jha, Deepak, Wozniak, Glenn G., Bridgers, Joseph B., Kerschner, Jenny L., Krajewski, Krzysztof, Martín, Glòria Mas, Morrison, Ashby J., Kutateladze, Tatiana G., Strahl, Brian D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2015
Materias:
Research Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4573853/
https://www.ncbi.nlm.nih.gov/pubmed/26341557
http://dx.doi.org/10.1101/gad.269977.115
Descripción
Sumario:The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.

Ejemplares similares