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Article: Identification of Histone deacetylase (HDAC)‐Associated Proteins with DNA‐Programmed Affinity Labeling

TitleIdentification of Histone deacetylase (HDAC)‐Associated Proteins with DNA‐Programmed Affinity Labeling
Authors
Keywordsaffinity probes
DNA-templated synthesis
histone deacetylases
photoaffinity labelling
protein–protein interactions
Issue Date2020
PublisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at https://onlinelibrary.wiley.com/journal/15213773
Citation
Angewandte Chemie (International Edition), 2020, v. 59 n. 40, p. 17525-17532 How to Cite?
AbstractHistone deacetylase (HDAC) is a major class of deacetylation enzymes. Many HDACs exist in large protein complexes in cells and their functions strongly depend on the complex composition. The identification of HDAC‐associated proteins is highly important in understanding their molecular mechanisms. Although affinity probes have been developed to study HDACs, they were mostly targeting the direct binder HDAC, while other proteins in the complex remain underexplored. We report a DNA‐based affinity labeling method capable of presenting different probe configurations without the need for preparing multiple probes. Using one binding probe, 9 probe configurations were created to profile HDAC complexes. Notably, this method identified indirect HDAC binders that may be inaccessible to traditional affinity probes, and it also revealed new biological implications for HDAC‐associated proteins. This study provided a simple and broadly applicable method for characterizing protein‐protein interactions.
Persistent Identifierhttp://hdl.handle.net/10722/288039
ISSN
2023 Impact Factor: 16.1
2023 SCImago Journal Rankings: 5.300
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhang, J-
dc.contributor.authorPeng, J-
dc.contributor.authorHuang, Y-
dc.contributor.authorMeng, L-
dc.contributor.authorLi, Q-
dc.contributor.authorXiong, F-
dc.contributor.authorLi, X-
dc.date.accessioned2020-10-05T12:06:58Z-
dc.date.available2020-10-05T12:06:58Z-
dc.date.issued2020-
dc.identifier.citationAngewandte Chemie (International Edition), 2020, v. 59 n. 40, p. 17525-17532-
dc.identifier.issn1433-7851-
dc.identifier.urihttp://hdl.handle.net/10722/288039-
dc.description.abstractHistone deacetylase (HDAC) is a major class of deacetylation enzymes. Many HDACs exist in large protein complexes in cells and their functions strongly depend on the complex composition. The identification of HDAC‐associated proteins is highly important in understanding their molecular mechanisms. Although affinity probes have been developed to study HDACs, they were mostly targeting the direct binder HDAC, while other proteins in the complex remain underexplored. We report a DNA‐based affinity labeling method capable of presenting different probe configurations without the need for preparing multiple probes. Using one binding probe, 9 probe configurations were created to profile HDAC complexes. Notably, this method identified indirect HDAC binders that may be inaccessible to traditional affinity probes, and it also revealed new biological implications for HDAC‐associated proteins. This study provided a simple and broadly applicable method for characterizing protein‐protein interactions.-
dc.languageeng-
dc.publisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at https://onlinelibrary.wiley.com/journal/15213773-
dc.relation.ispartofAngewandte Chemie (International Edition)-
dc.rightsThis is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.-
dc.subjectaffinity probes-
dc.subjectDNA-templated synthesis-
dc.subjecthistone deacetylases-
dc.subjectphotoaffinity labelling-
dc.subjectprotein–protein interactions-
dc.titleIdentification of Histone deacetylase (HDAC)‐Associated Proteins with DNA‐Programmed Affinity Labeling-
dc.typeArticle-
dc.identifier.emailZhang, J: chembiol@HKUCC-COM.hku.hk-
dc.identifier.emailHuang, Y: huangyr0@hku.hk-
dc.identifier.emailLi, X: xiaoyuli@hku.hk-
dc.identifier.authorityLi, X=rp02080-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/anie.202001205-
dc.identifier.pmid32613694-
dc.identifier.scopuseid_2-s2.0-85089257345-
dc.identifier.hkuros315337-
dc.identifier.volume59-
dc.identifier.issue40-
dc.identifier.spage17525-
dc.identifier.epage17532-
dc.identifier.isiWOS:000557983300001-
dc.publisher.placeGermany-
dc.identifier.issnl1433-7851-

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