HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
Once DNA breaks occur, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other DNA repair factors to initiate the repair process. Here, the authors resolve the crystal structures of mouse and human HPF1, and human HPF1/PARP1 complex proving insights into PARP1 regulation.
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Nature Portfolio
2021
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oai:doaj.org-article:5521b4d0d2ee4c4d8454f7128bbf80472021-12-02T14:21:24ZHPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones10.1038/s41467-021-21302-42041-1723https://doaj.org/article/5521b4d0d2ee4c4d8454f7128bbf80472021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21302-4https://doaj.org/toc/2041-1723Once DNA breaks occur, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other DNA repair factors to initiate the repair process. Here, the authors resolve the crystal structures of mouse and human HPF1, and human HPF1/PARP1 complex proving insights into PARP1 regulation.Fa-Hui SunPeng ZhaoNan ZhangLu-Lu KongCatherine C. L. WongCai-Hong YunNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021) |
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Science Q Fa-Hui Sun Peng Zhao Nan Zhang Lu-Lu Kong Catherine C. L. Wong Cai-Hong Yun HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
description |
Once DNA breaks occur, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other DNA repair factors to initiate the repair process. Here, the authors resolve the crystal structures of mouse and human HPF1, and human HPF1/PARP1 complex proving insights into PARP1 regulation. |
format |
article |
author |
Fa-Hui Sun Peng Zhao Nan Zhang Lu-Lu Kong Catherine C. L. Wong Cai-Hong Yun |
author_facet |
Fa-Hui Sun Peng Zhao Nan Zhang Lu-Lu Kong Catherine C. L. Wong Cai-Hong Yun |
author_sort |
Fa-Hui Sun |
title |
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
title_short |
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
title_full |
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
title_fullStr |
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
title_full_unstemmed |
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones |
title_sort |
hpf1 remodels the active site of parp1 to enable the serine adp-ribosylation of histones |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/5521b4d0d2ee4c4d8454f7128bbf8047 |
work_keys_str_mv |
AT fahuisun hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones AT pengzhao hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones AT nanzhang hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones AT lulukong hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones AT catherineclwong hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones AT caihongyun hpf1remodelstheactivesiteofparp1toenabletheserineadpribosylationofhistones |
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