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ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair
RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization an...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5794780/ https://www.ncbi.nlm.nih.gov/pubmed/29391496 http://dx.doi.org/10.1038/s41598-018-20557-0 |
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author | Tang, Qun Liu, Yan-Ping Shan, Hai-Huan Tian, Li-Fei Zhang, Jie-Zhong Yan, Xiao-Xue |
author_facet | Tang, Qun Liu, Yan-Ping Shan, Hai-Huan Tian, Li-Fei Zhang, Jie-Zhong Yan, Xiao-Xue |
author_sort | Tang, Qun |
collection | PubMed |
description | RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization and structural homology with Rad50 and SMC proteins. However, the mechanism and action pattern of RecF ATP-dependent dimerization remains unclear. Here, We determined three crystal structures of TTERecF, TTERecF-ATP and TTERecF-ATPɤS from Thermoanaerobacter tengcongensis that reveal a novel ATP-driven RecF dimerization. RecF contains a positively charged tunnel on its dimer interface that is essential to ATP binding. Our structural and biochemical data indicate that the Walker A motif serves as a switch and plays a key role in ATP binding and RecF dimerization. Furthermore, Biolayer interferometry assay results showed that the TTERecF interacted with ATP and formed a dimer, displaying a higher affinity for DNA than that of the TTERecF monomer. Overall, our results provide a solid structural basis for understanding the process of RecF binding with ATP and the functional mechanism of ATP-dependent RecF dimerization. |
format | Online Article Text |
id | pubmed-5794780 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-57947802018-02-12 ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair Tang, Qun Liu, Yan-Ping Shan, Hai-Huan Tian, Li-Fei Zhang, Jie-Zhong Yan, Xiao-Xue Sci Rep Article RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization and structural homology with Rad50 and SMC proteins. However, the mechanism and action pattern of RecF ATP-dependent dimerization remains unclear. Here, We determined three crystal structures of TTERecF, TTERecF-ATP and TTERecF-ATPɤS from Thermoanaerobacter tengcongensis that reveal a novel ATP-driven RecF dimerization. RecF contains a positively charged tunnel on its dimer interface that is essential to ATP binding. Our structural and biochemical data indicate that the Walker A motif serves as a switch and plays a key role in ATP binding and RecF dimerization. Furthermore, Biolayer interferometry assay results showed that the TTERecF interacted with ATP and formed a dimer, displaying a higher affinity for DNA than that of the TTERecF monomer. Overall, our results provide a solid structural basis for understanding the process of RecF binding with ATP and the functional mechanism of ATP-dependent RecF dimerization. Nature Publishing Group UK 2018-02-01 /pmc/articles/PMC5794780/ /pubmed/29391496 http://dx.doi.org/10.1038/s41598-018-20557-0 Text en © The Author(s) 2018 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/. |
spellingShingle | Article Tang, Qun Liu, Yan-Ping Shan, Hai-Huan Tian, Li-Fei Zhang, Jie-Zhong Yan, Xiao-Xue ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title | ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title_full | ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title_fullStr | ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title_full_unstemmed | ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title_short | ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair |
title_sort | atp-dependent conformational change in abc-atpase recf serves as a switch in dna repair |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5794780/ https://www.ncbi.nlm.nih.gov/pubmed/29391496 http://dx.doi.org/10.1038/s41598-018-20557-0 |
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