Hot on RAD51C: structure and functions of RAD51C‐XRCC3

A new study by Longo, Roy et al. has solved the structure of the RAD51C‐XRCC3 (CX3) heterodimer with a bound ATP analog, identifying two main structural interfaces and defining separable replication fork stability roles. One function relates to the ability of RAD51C to bind and assemble CX3 on nasce...

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Detalles Bibliográficos
Autores principales: Szakal, Barnabas, Branzei, Dana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Commentary
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10552886/
https://www.ncbi.nlm.nih.gov/pubmed/37681281
http://dx.doi.org/10.1002/1878-0261.13518
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author Szakal, Barnabas
Branzei, Dana
author_facet Szakal, Barnabas
Branzei, Dana
author_sort Szakal, Barnabas
collection PubMed
description A new study by Longo, Roy et al. has solved the structure of the RAD51C‐XRCC3 (CX3) heterodimer with a bound ATP analog, identifying two main structural interfaces and defining separable replication fork stability roles. One function relates to the ability of RAD51C to bind and assemble CX3 on nascent DNA, with an impact on the ability of forks to restart upon replication stress. The other relates to effective CX3 heterodimer formation, required for 5′ RAD51 filament capping, with effects on RAD51 filament disassembly, fork protection and influencing the persistence of reversed forks.
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spelling pubmed-105528862023-10-06 Hot on RAD51C: structure and functions of RAD51C‐XRCC3 Szakal, Barnabas Branzei, Dana Mol Oncol Commentary A new study by Longo, Roy et al. has solved the structure of the RAD51C‐XRCC3 (CX3) heterodimer with a bound ATP analog, identifying two main structural interfaces and defining separable replication fork stability roles. One function relates to the ability of RAD51C to bind and assemble CX3 on nascent DNA, with an impact on the ability of forks to restart upon replication stress. The other relates to effective CX3 heterodimer formation, required for 5′ RAD51 filament capping, with effects on RAD51 filament disassembly, fork protection and influencing the persistence of reversed forks. John Wiley and Sons Inc. 2023-09-11 /pmc/articles/PMC10552886/ /pubmed/37681281 http://dx.doi.org/10.1002/1878-0261.13518 Text en © 2023 The Authors. Molecular Oncology published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Szakal, Barnabas
Branzei, Dana
Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title_full Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title_fullStr Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title_full_unstemmed Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title_short Hot on RAD51C: structure and functions of RAD51C‐XRCC3
title_sort hot on rad51c: structure and functions of rad51c‐xrcc3
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10552886/
https://www.ncbi.nlm.nih.gov/pubmed/37681281
http://dx.doi.org/10.1002/1878-0261.13518
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