Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling

The demethylase activity of KDM5A is allosterically enhanced by binding of histone H3 to its PHD1 reader domain, through an unknown mechanism. Here the authors show that the PHD1 domain drives ligand-induced allosteric stimulation by stabilizing the binding of substrate to the catalytic domain.

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Autores principales:	James E. Longbotham, Cynthia M. Chio, Venkatasubramanian Dharmarajan, Michael J. Trnka, Idelisse Ortiz Torres, Devrishi Goswami, Karen Ruiz, Alma L. Burlingame, Patrick R. Griffin, Danica Galonić Fujimori
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8af366d414d64557aaf7cda67d5a31e7
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spelling	oai:doaj.org-article:8af366d414d64557aaf7cda67d5a31e72021-12-02T15:35:06ZHistone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling10.1038/s41467-018-07829-z2041-1723https://doaj.org/article/8af366d414d64557aaf7cda67d5a31e72019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07829-zhttps://doaj.org/toc/2041-1723The demethylase activity of KDM5A is allosterically enhanced by binding of histone H3 to its PHD1 reader domain, through an unknown mechanism. Here the authors show that the PHD1 domain drives ligand-induced allosteric stimulation by stabilizing the binding of substrate to the catalytic domain.James E. LongbothamCynthia M. ChioVenkatasubramanian DharmarajanMichael J. TrnkaIdelisse Ortiz TorresDevrishi GoswamiKaren RuizAlma L. BurlingamePatrick R. GriffinDanica Galonić FujimoriNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q James E. Longbotham Cynthia M. Chio Venkatasubramanian Dharmarajan Michael J. Trnka Idelisse Ortiz Torres Devrishi Goswami Karen Ruiz Alma L. Burlingame Patrick R. Griffin Danica Galonić Fujimori Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
description	The demethylase activity of KDM5A is allosterically enhanced by binding of histone H3 to its PHD1 reader domain, through an unknown mechanism. Here the authors show that the PHD1 domain drives ligand-induced allosteric stimulation by stabilizing the binding of substrate to the catalytic domain.
format	article
author	James E. Longbotham Cynthia M. Chio Venkatasubramanian Dharmarajan Michael J. Trnka Idelisse Ortiz Torres Devrishi Goswami Karen Ruiz Alma L. Burlingame Patrick R. Griffin Danica Galonić Fujimori
author_facet	James E. Longbotham Cynthia M. Chio Venkatasubramanian Dharmarajan Michael J. Trnka Idelisse Ortiz Torres Devrishi Goswami Karen Ruiz Alma L. Burlingame Patrick R. Griffin Danica Galonić Fujimori
author_sort	James E. Longbotham
title	Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
title_short	Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
title_full	Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
title_fullStr	Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
title_full_unstemmed	Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
title_sort	histone h3 binding to the phd1 domain of histone demethylase kdm5a enables active site remodeling
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/8af366d414d64557aaf7cda67d5a31e7
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Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling

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