Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination

Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination

Histone ubiquitination plays a critical role in the DNA damage response pathway. Here the authors reveal how RNF168 ubiquitinates the H2A family including noncanonical variants, H2AZ and macroH2A1/2, at the divergent N-terminal tail lysine residue.

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Autores principales: Jessica L. Kelliher, Kirk L. West, Qingguo Gong, Justin W. C. Leung
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Q
Acceso en línea:https://doaj.org/article/78f4cd1bfa81402db000d570e1f392c6
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spelling oai:doaj.org-article:78f4cd1bfa81402db000d570e1f392c62021-12-02T16:51:08ZHistone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination10.1038/s41467-020-16307-42041-1723https://doaj.org/article/78f4cd1bfa81402db000d570e1f392c62020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16307-4https://doaj.org/toc/2041-1723Histone ubiquitination plays a critical role in the DNA damage response pathway. Here the authors reveal how RNF168 ubiquitinates the H2A family including noncanonical variants, H2AZ and macroH2A1/2, at the divergent N-terminal tail lysine residue.Jessica L. KelliherKirk L. WestQingguo GongJustin W. C. LeungNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jessica L. Kelliher
Kirk L. West
Qingguo Gong
Justin W. C. Leung
Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
description Histone ubiquitination plays a critical role in the DNA damage response pathway. Here the authors reveal how RNF168 ubiquitinates the H2A family including noncanonical variants, H2AZ and macroH2A1/2, at the divergent N-terminal tail lysine residue.
format article
author Jessica L. Kelliher
Kirk L. West
Qingguo Gong
Justin W. C. Leung
author_facet Jessica L. Kelliher
Kirk L. West
Qingguo Gong
Justin W. C. Leung
author_sort Jessica L. Kelliher
title Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
title_short Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
title_full Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
title_fullStr Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
title_full_unstemmed Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination
title_sort histone h2a variants alpha1-extension helix directs rnf168-mediated ubiquitination
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/78f4cd1bfa81402db000d570e1f392c6
work_keys_str_mv AT jessicalkelliher histoneh2avariantsalpha1extensionhelixdirectsrnf168mediatedubiquitination
AT kirklwest histoneh2avariantsalpha1extensionhelixdirectsrnf168mediatedubiquitination
AT qingguogong histoneh2avariantsalpha1extensionhelixdirectsrnf168mediatedubiquitination
AT justinwcleung histoneh2avariantsalpha1extensionhelixdirectsrnf168mediatedubiquitination
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