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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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
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author Klein, Brianna J.
Cox, Khan L.
Jang, Suk Min
Singh, Rohit K.
Côté, Jacques
Poirier, Michael G.
Kutateladze, Tatiana G.
author_facet Klein, Brianna J.
Cox, Khan L.
Jang, Suk Min
Singh, Rohit K.
Côté, Jacques
Poirier, Michael G.
Kutateladze, Tatiana G.
author_sort Klein, Brianna J.
collection PubMed
description 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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spelling pubmed-80822622021-05-11 Structural and biophysical characterization of the nucleosome-binding PZP domain Klein, Brianna J. Cox, Khan L. Jang, Suk Min Singh, Rohit K. Côté, Jacques Poirier, Michael G. Kutateladze, Tatiana G. STAR Protoc Protocol 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). Elsevier 2021-04-19 /pmc/articles/PMC8082262/ /pubmed/33982013 http://dx.doi.org/10.1016/j.xpro.2021.100479 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Klein, Brianna J.
Cox, Khan L.
Jang, Suk Min
Singh, Rohit K.
Côté, Jacques
Poirier, Michael G.
Kutateladze, Tatiana G.
Structural and biophysical characterization of the nucleosome-binding PZP domain
title Structural and biophysical characterization of the nucleosome-binding PZP domain
title_full Structural and biophysical characterization of the nucleosome-binding PZP domain
title_fullStr Structural and biophysical characterization of the nucleosome-binding PZP domain
title_full_unstemmed Structural and biophysical characterization of the nucleosome-binding PZP domain
title_short Structural and biophysical characterization of the nucleosome-binding PZP domain
title_sort structural and biophysical characterization of the nucleosome-binding pzp domain
topic Protocol
url 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
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