The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations
The DNA helicase ASCC3 is the largest subunit of the activating signal co-integrator complex (ASCC), and its DNA unwinding activity is required for the AlkBH3/ASCC-dependent DNA de-alkylation repair pathway. Here, the authors identify a minimal stable complex of the two ASCC subunits ASCC2 and ASCC3...
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Nature Portfolio
2020
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oai:doaj.org-article:d118f2503a854806ab453466797e9c862021-12-02T14:42:14ZThe interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations10.1038/s41467-020-19221-x2041-1723https://doaj.org/article/d118f2503a854806ab453466797e9c862020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19221-xhttps://doaj.org/toc/2041-1723The DNA helicase ASCC3 is the largest subunit of the activating signal co-integrator complex (ASCC), and its DNA unwinding activity is required for the AlkBH3/ASCC-dependent DNA de-alkylation repair pathway. Here, the authors identify a minimal stable complex of the two ASCC subunits ASCC2 and ASCC3, determine the complex crystal structure and further show that cancer-related mutations at the interface between both proteins reduce ASCC2–ASCC3 affinity.Junqiao JiaEva AbsmeierNicole HoltonAgnieszka J. Pietrzyk-BrzezinskaPhilipp HackertKatherine E. BohnsackMarkus T. BohnsackMarkus C. WahlNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020) |
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Science Q Junqiao Jia Eva Absmeier Nicole Holton Agnieszka J. Pietrzyk-Brzezinska Philipp Hackert Katherine E. Bohnsack Markus T. Bohnsack Markus C. Wahl The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
description |
The DNA helicase ASCC3 is the largest subunit of the activating signal co-integrator complex (ASCC), and its DNA unwinding activity is required for the AlkBH3/ASCC-dependent DNA de-alkylation repair pathway. Here, the authors identify a minimal stable complex of the two ASCC subunits ASCC2 and ASCC3, determine the complex crystal structure and further show that cancer-related mutations at the interface between both proteins reduce ASCC2–ASCC3 affinity. |
format |
article |
author |
Junqiao Jia Eva Absmeier Nicole Holton Agnieszka J. Pietrzyk-Brzezinska Philipp Hackert Katherine E. Bohnsack Markus T. Bohnsack Markus C. Wahl |
author_facet |
Junqiao Jia Eva Absmeier Nicole Holton Agnieszka J. Pietrzyk-Brzezinska Philipp Hackert Katherine E. Bohnsack Markus T. Bohnsack Markus C. Wahl |
author_sort |
Junqiao Jia |
title |
The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
title_short |
The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
title_full |
The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
title_fullStr |
The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
title_full_unstemmed |
The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations |
title_sort |
interaction of dna repair factors ascc2 and ascc3 is affected by somatic cancer mutations |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/d118f2503a854806ab453466797e9c86 |
work_keys_str_mv |
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