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Structural and biophysical characterization of the nucleosome-binding PZP domain.

ABSTRACT: 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).

SUBMITTER: Klein BJ

PROVIDER: S-EPMC8082262 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature

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Structural and biophysical characterization of the nucleosome-binding PZP domain.

Klein Brianna J BJ Cox Khan L KL Jang Suk Min SM Singh Rohit K RK Côté Jacques J Poirier Michael G MG Kutateladze Tatiana G TG

STAR protocols 20210419 2

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 (BRPF1PZP). BRPF1PZP 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 BRPF1PZP, H3 ta ...[more]

PMID: 33982013

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