Abstract

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 breaks1. 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 structures2,3 now put the issue beyond doubt.

Recent structures of DNA-bound bacterial and phage recombinases provide insights into homologous recombination and suggest relation to the eukaryotic Rad52 and identification of a Rad52 single strand annealing protein (SSAP) superfamily.

Details

Title
The Rad52 SSAP superfamily and new insight into homologous recombination
Author
Al-Fatlawi, Ali 1 ; Schroeder, Michael 1   VIAFID ORCID Logo  ; Stewart, A. Francis 2   VIAFID ORCID Logo 

1  Technische Universität Dresden, Biotechnology Center, Center for Molecular and Cellular Bioengineering, Dresden, Germany (GRID:grid.4488.0) (ISNI:0000 0001 2111 7257) 
2  Technische Universität Dresden, Biotechnology Center, Center for Molecular and Cellular Bioengineering, Dresden, Germany (GRID:grid.4488.0) (ISNI:0000 0001 2111 7257); University of New South Wales, School of Biotechnology and Biomolecular Sciences, Sydney, Australia (GRID:grid.1005.4) (ISNI:0000 0004 4902 0432) 
Pages
87
Publication year
2023
Publication date
2023
Publisher
Nature Publishing Group
e-ISSN
23993642
Source type
Scholarly Journal
Language of publication
English
DOI
https://doi.org/10.1038/s42003-023-04476-z
ProQuest document ID
2768595697
Copyright
© The Author(s) 2023. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.