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Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics

Lysine succinylation is a recently discovered posttranslational modification that plays critical roles in metabolism, epigenetic signaling, and human diseases. To investigate the effects of site-specific histone lysine succinylation on nucleosome dynamics requires the generation of homogeneously mod...

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Detalles Bibliográficos
Autores principales: Jing, Yihang, Liu, Zheng, Li, Xiang David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8215284/
https://www.ncbi.nlm.nih.gov/pubmed/34189470
http://dx.doi.org/10.1016/j.xpro.2021.100604
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author Jing, Yihang
Liu, Zheng
Li, Xiang David
author_facet Jing, Yihang
Liu, Zheng
Li, Xiang David
author_sort Jing, Yihang
collection PubMed
description Lysine succinylation is a recently discovered posttranslational modification that plays critical roles in metabolism, epigenetic signaling, and human diseases. To investigate the effects of site-specific histone lysine succinylation on nucleosome dynamics requires the generation of homogeneously modified histones, which is a significant challenge. Here, we report a protocol for the rapid site-specific installation of a succinyl lysine analog onto histone. We then use a Förster resonance energy transfer approach to characterize the impact on nucleosome dynamics. For complete details on the use and execution of this protocol, please refer to Jing et al. (2018).
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spelling pubmed-82152842021-06-28 Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics Jing, Yihang Liu, Zheng Li, Xiang David STAR Protoc Protocol Lysine succinylation is a recently discovered posttranslational modification that plays critical roles in metabolism, epigenetic signaling, and human diseases. To investigate the effects of site-specific histone lysine succinylation on nucleosome dynamics requires the generation of homogeneously modified histones, which is a significant challenge. Here, we report a protocol for the rapid site-specific installation of a succinyl lysine analog onto histone. We then use a Förster resonance energy transfer approach to characterize the impact on nucleosome dynamics. For complete details on the use and execution of this protocol, please refer to Jing et al. (2018). Elsevier 2021-06-12 /pmc/articles/PMC8215284/ /pubmed/34189470 http://dx.doi.org/10.1016/j.xpro.2021.100604 Text en © 2021 The Authors 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
Jing, Yihang
Liu, Zheng
Li, Xiang David
Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title_full Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title_fullStr Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title_full_unstemmed Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title_short Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
title_sort protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8215284/
https://www.ncbi.nlm.nih.gov/pubmed/34189470
http://dx.doi.org/10.1016/j.xpro.2021.100604
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