The Rad52 SSAP superfamily and new insight into homologous recombination

Rad52 is a highly conserved eukaryotic protein that can mediate the annealing of complementary DNA strands to initiate homologous recombination for the repair of double-strand breaks(1). Suspicions that at least some prokaryotic single-strand annealing proteins (SSAPs) are related to Rad52 have been...

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Autores principales: Al-Fatlawi, Ali, Schroeder, Michael, Stewart, A. Francis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Comment
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9870868/
https://www.ncbi.nlm.nih.gov/pubmed/36690694
http://dx.doi.org/10.1038/s42003-023-04476-z
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author Al-Fatlawi, Ali
Schroeder, Michael
Stewart, A. Francis
author_facet Al-Fatlawi, Ali
Schroeder, Michael
Stewart, A. Francis
author_sort Al-Fatlawi, Ali
collection PubMed
description Rad52 is a highly conserved eukaryotic protein that can mediate the annealing of complementary DNA strands to initiate homologous recombination for the repair of double-strand breaks(1). Suspicions that at least some prokaryotic single-strand annealing proteins (SSAPs) are related to Rad52 have been discussed for more than two decades. Two recent cryo-EM structures(2,3) now put the issue beyond doubt.
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spelling pubmed-98708682023-01-25 The Rad52 SSAP superfamily and new insight into homologous recombination Al-Fatlawi, Ali Schroeder, Michael Stewart, A. Francis Commun Biol Comment Rad52 is a highly conserved eukaryotic protein that can mediate the annealing of complementary DNA strands to initiate homologous recombination for the repair of double-strand breaks(1). Suspicions that at least some prokaryotic single-strand annealing proteins (SSAPs) are related to Rad52 have been discussed for more than two decades. Two recent cryo-EM structures(2,3) now put the issue beyond doubt. Nature Publishing Group UK 2023-01-23 /pmc/articles/PMC9870868/ /pubmed/36690694 http://dx.doi.org/10.1038/s42003-023-04476-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Comment
Al-Fatlawi, Ali
Schroeder, Michael
Stewart, A. Francis
The Rad52 SSAP superfamily and new insight into homologous recombination
title The Rad52 SSAP superfamily and new insight into homologous recombination
title_full The Rad52 SSAP superfamily and new insight into homologous recombination
title_fullStr The Rad52 SSAP superfamily and new insight into homologous recombination
title_full_unstemmed The Rad52 SSAP superfamily and new insight into homologous recombination
title_short The Rad52 SSAP superfamily and new insight into homologous recombination
title_sort rad52 ssap superfamily and new insight into homologous recombination
topic Comment
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9870868/
https://www.ncbi.nlm.nih.gov/pubmed/36690694
http://dx.doi.org/10.1038/s42003-023-04476-z
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