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Article: Development of multifunctional synthetic nucleosomes to interrogate chromatin-mediated protein interactions

TitleDevelopment of multifunctional synthetic nucleosomes to interrogate chromatin-mediated protein interactions
Authors
Issue Date3-May-2023
PublisherAmerican Association for the Advancement of Science
Citation
Science Advances, 2023, v. 9, n. 18 How to Cite?
Abstract

Various proteins bind to chromatin to regulate DNA and its associated processes such as replication, transcription, and damage repair. The identification and characterization of these chromatin-associating proteins remain a challenge, as their interactions with chromatin often occur within the context of the local nucleosome or chromatin structure, which makes conventional peptide-based strategies unsuitable. Here, we developed a simple and robust protein labeling chemistry to prepare synthetic multifunctional nucleosomes that carry a photoreactive group, a biorthogonal handle, and a disulfide moiety to examine chromatin-protein interactions in a nucleosomal context. Using the prepared protein- and nucleosome-based photoaffinity probes, we examined a number of protein-protein and protein-nucleosome interactions. In particular, we (i) mapped the binding sites for the HMGN2-nucleosome interaction, (ii) provided the evidence for transition between the active and poised states of DOT1L in recognizing H3K79 within the nucleosome, and (iii) identified OARD1 and LAP2α as nucleosome acidic patch-associating proteins. This study provides powerful and versatile chemical tools for interrogating chromatin-associating proteins.


Persistent Identifierhttp://hdl.handle.net/10722/331700
ISSN
2023 Impact Factor: 11.7
2023 SCImago Journal Rankings: 4.483
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Zheng-
dc.contributor.authorWu, Yiping-
dc.contributor.authorMao, Xin-
dc.contributor.authorKwan, Ka Chun Jonathan-
dc.contributor.authorCheng, Xinxin-
dc.contributor.authorLi, Xin-
dc.contributor.authorJing, Yihang-
dc.contributor.authorLi, Xiang David-
dc.date.accessioned2023-09-21T06:58:08Z-
dc.date.available2023-09-21T06:58:08Z-
dc.date.issued2023-05-03-
dc.identifier.citationScience Advances, 2023, v. 9, n. 18-
dc.identifier.issn2375-2548-
dc.identifier.urihttp://hdl.handle.net/10722/331700-
dc.description.abstract<p>Various proteins bind to chromatin to regulate DNA and its associated processes such as replication, transcription, and damage repair. The identification and characterization of these chromatin-associating proteins remain a challenge, as their interactions with chromatin often occur within the context of the local nucleosome or chromatin structure, which makes conventional peptide-based strategies unsuitable. Here, we developed a simple and robust protein labeling chemistry to prepare synthetic multifunctional nucleosomes that carry a photoreactive group, a biorthogonal handle, and a disulfide moiety to examine chromatin-protein interactions in a nucleosomal context. Using the prepared protein- and nucleosome-based photoaffinity probes, we examined a number of protein-protein and protein-nucleosome interactions. In particular, we (i) mapped the binding sites for the HMGN2-nucleosome interaction, (ii) provided the evidence for transition between the active and poised states of DOT1L in recognizing H3K79 within the nucleosome, and (iii) identified OARD1 and LAP2α as nucleosome acidic patch-associating proteins. This study provides powerful and versatile chemical tools for interrogating chromatin-associating proteins.</p>-
dc.languageeng-
dc.publisherAmerican Association for the Advancement of Science-
dc.relation.ispartofScience Advances-
dc.titleDevelopment of multifunctional synthetic nucleosomes to interrogate chromatin-mediated protein interactions-
dc.typeArticle-
dc.identifier.doi10.1126/sciadv.ade5186-
dc.identifier.scopuseid_2-s2.0-85159548115-
dc.identifier.volume9-
dc.identifier.issue18-
dc.identifier.eissn2375-2548-
dc.identifier.isiWOS:000988268100016-
dc.identifier.issnl2375-2548-

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