دورية أكاديمية
أعرض في EDS

Exploring the Ligand Preferences of the PHD1 Domain of Histone Demethylase KDM5A Reveals Tolerance for Modifications of the Q5 Residue of Histone 3.

التفاصيل البيبلوغرافية
العنوان: Exploring the Ligand Preferences of the PHD1 Domain of Histone Demethylase KDM5A Reveals Tolerance for Modifications of the Q5 Residue of Histone 3.
المؤلفون: Anderson SE; Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States., Longbotham JE; Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, California 94158, United States., O'Kane PT; Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States., Ugur FS; Chemistry and Chemical Biology Graduate Program, University of California San Francisco, San Francisco, California 94158, United States., Fujimori DG; Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, California 94158, United States.; Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.; Quantitative Biosciences Institute, University of California San Francisco, San Francisco, California 94158, United States., Mrksich M; Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States.; Department of Biomedical Engineering, Northwestern University, Evanston, Illinois 60208, United States.; Department of Cell and Developmental Biology, Northwestern University, Evanston, Illinois 60208, United States.
المصدر: ACS chemical biology [ACS Chem Biol] 2021 Jan 15; Vol. 16 (1), pp. 205-213. Date of Electronic Publication: 2020 Dec 14.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101282906 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1554-8937 (Electronic) Linking ISSN: 15548929 NLM ISO Abbreviation: ACS Chem Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c2006-
مواضيع طبية MeSH: Histones/*metabolism , Hypoxia-Inducible Factor-Proline Dioxygenases/*metabolism , Retinoblastoma-Binding Protein 2/*metabolism, Fluorescence Polarization ; Humans ; Ligands
مستخلص: Understanding the ligand preferences of epigenetic reader domains enables identification of modification states of chromatin with which these domains associate and can yield insight into recruitment and catalysis of chromatin-acting complexes. However, thorough exploration of the ligand preferences of reader domains is hindered by the limitations of traditional protein-ligand binding assays. Here, we evaluate the binding preferences of the PHD1 domain of histone demethylase KDM5A using the protein interaction by SAMDI (PI-SAMDI) assay, which measures protein-ligand binding in a high-throughput and sensitive manner via binding-induced enhancement in the activity of a reporter enzyme, in combination with fluorescence polarization. The PI-SAMDI assay was validated by confirming its ability to accurately profile the relative binding affinity of a set of well-characterized histone 3 (H3) ligands of PHD1. The assay was then used to assess the affinity of PHD1 for 361 H3 mutant ligands, a select number of which were further characterized by fluorescence polarization. Together, these experiments revealed PHD1's tolerance for H3Q5 mutations, including an unexpected tolerance for aromatic residues in this position. Motivated by this finding, we further demonstrate a high-affinity interaction between PHD1 and recently identified Q5-serotonylated H3. This work yields interesting insights into permissible PHD1-H3 interactions and demonstrates the value of interfacing PI-SAMDI and fluorescence polarization in investigations of protein-ligand binding.
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معلومات مُعتمدة: R01 GM114044 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Histones)
0 (Ligands)
EC 1.14.11.- (KDM5A protein, human)
EC 1.14.11.27 (Retinoblastoma-Binding Protein 2)
EC 1.14.11.29 (EGLN2 protein, human)
EC 1.14.11.29 (Hypoxia-Inducible Factor-Proline Dioxygenases)
تواريخ الأحداث: Date Created: 20201214 Date Completed: 20210707 Latest Revision: 20240402
رمز التحديث: 20240402
مُعرف محوري في PubMed: PMC8168426
DOI: 10.1021/acschembio.0c00891
PMID: 33314922
قاعدة البيانات: MEDLINE
الوصف
تدمد:1554-8937
DOI:10.1021/acschembio.0c00891