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- Publisher Website: 10.1021/acschembio.4c00240
- Scopus: eid_2-s2.0-85195319573
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Article: Genetically Encoded Epitope Tag for Probing Lysine Acylation-Mediated Protein–Protein Interactions
Title | Genetically Encoded Epitope Tag for Probing Lysine Acylation-Mediated Protein–Protein Interactions |
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Authors | |
Issue Date | 3-Jun-2024 |
Publisher | American Chemical Society |
Citation | ACS Chemical Biology, 2024, v. 19, n. 6, p. 1376-1386 How to Cite? |
Abstract | Histone lysine acetylation (Kac) and crotonylation (Kcr) marks mediate the recruitment of YEATS domains to chromatin. In this way, YEATS domain-containing proteins such as AF9 participate in the regulation of DNA-templated processes. Our previous study showed that the replacement of Kac/Kcr by a 2-furancarbonyllysine (Kfu) residue led to greatly enhanced affinity toward the AF9 YEATS domain, rendering Kfu-containing peptides useful chemical tools to probe the AF9 YEATS–Kac/Kcr interactions. Here, we report the genetic incorporation of Kfu in Escherichia coli and mammalian cells through the amber codon suppression technology. We develop a Kfu-containing epitope tag, termed RAY-tag, which can robustly and selectively engage with the AF9 YEATS domain in vitro and in cellulo. We further demonstrate that the fusion of RAY-tag to different protein modules, including fluorescent proteins and DNA binding proteins, can facilitate the interrogation of the histone lysine acylation-mediated recruitment of the AF9 YEATS domain in different biological contexts. |
Persistent Identifier | http://hdl.handle.net/10722/346231 |
ISSN | 2023 Impact Factor: 3.5 2023 SCImago Journal Rankings: 1.344 |
DC Field | Value | Language |
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dc.contributor.author | Tian, Gaofei | - |
dc.contributor.author | Li, Xin | - |
dc.contributor.author | Li, Xiang David | - |
dc.date.accessioned | 2024-09-12T00:31:00Z | - |
dc.date.available | 2024-09-12T00:31:00Z | - |
dc.date.issued | 2024-06-03 | - |
dc.identifier.citation | ACS Chemical Biology, 2024, v. 19, n. 6, p. 1376-1386 | - |
dc.identifier.issn | 1554-8929 | - |
dc.identifier.uri | http://hdl.handle.net/10722/346231 | - |
dc.description.abstract | <p>Histone lysine acetylation (Kac) and crotonylation (Kcr) marks mediate the recruitment of YEATS domains to chromatin. In this way, YEATS domain-containing proteins such as AF9 participate in the regulation of DNA-templated processes. Our previous study showed that the replacement of Kac/Kcr by a 2-furancarbonyllysine (Kfu) residue led to greatly enhanced affinity toward the AF9 YEATS domain, rendering Kfu-containing peptides useful chemical tools to probe the AF9 YEATS–Kac/Kcr interactions. Here, we report the genetic incorporation of Kfu in <em>Escherichia coli</em> and mammalian cells through the amber codon suppression technology. We develop a Kfu-containing epitope tag, termed RAY-tag, which can robustly and selectively engage with the AF9 YEATS domain <em>in vitro</em> and <em>in cellulo</em>. We further demonstrate that the fusion of RAY-tag to different protein modules, including fluorescent proteins and DNA binding proteins, can facilitate the interrogation of the histone lysine acylation-mediated recruitment of the AF9 YEATS domain in different biological contexts.</p> | - |
dc.language | eng | - |
dc.publisher | American Chemical Society | - |
dc.relation.ispartof | ACS Chemical Biology | - |
dc.title | Genetically Encoded Epitope Tag for Probing Lysine Acylation-Mediated Protein–Protein Interactions | - |
dc.type | Article | - |
dc.identifier.doi | 10.1021/acschembio.4c00240 | - |
dc.identifier.scopus | eid_2-s2.0-85195319573 | - |
dc.identifier.volume | 19 | - |
dc.identifier.issue | 6 | - |
dc.identifier.spage | 1376 | - |
dc.identifier.epage | 1386 | - |
dc.identifier.eissn | 1554-8937 | - |
dc.identifier.issnl | 1554-8929 | - |