Structural and biophysical characterization of the nucleosome-binding PZP domain

The core subunit of the MORF acetyltransferase complex BRPF1 contains a unique combination of zinc fingers, including a plant homeodomain (PHD) finger followed by a zinc knuckle and another PHD finger, which together form a PZP domain (BRPF1(PZP)). BRPF1(PZP) has been shown to bind to the nucleosome...

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Detalles Bibliográficos
Autores principales: Klein, Brianna J., Cox, Khan L., Jang, Suk Min, Singh, Rohit K., Côté, Jacques, Poirier, Michael G., Kutateladze, Tatiana G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Protocol
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8082262/
https://www.ncbi.nlm.nih.gov/pubmed/33982013
http://dx.doi.org/10.1016/j.xpro.2021.100479
Descripción
Sumario:The core subunit of the MORF acetyltransferase complex BRPF1 contains a unique combination of zinc fingers, including a plant homeodomain (PHD) finger followed by a zinc knuckle and another PHD finger, which together form a PZP domain (BRPF1(PZP)). BRPF1(PZP) has been shown to bind to the nucleosome and make contacts with both histone H3 tail and DNA. Here, we describe biophysical and structural methods for characterization of the interactions between BRPF1(PZP), H3 tail, DNA, and the intact nucleosome. For complete details on the use and execution of this protocol, please refer to Klein et al. (2020).

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