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Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA
Deinococcus radiodurans (Dr) has one of the most robust DNA repair systems, which is capable of withstanding extreme doses of ionizing radiation and other sources of DNA damage. DrRecA, a central enzyme of recombinational DNA repair, is essential for extreme radioresistance. In the presence of ATP,...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7583915/ https://www.ncbi.nlm.nih.gov/pubmed/33036395 http://dx.doi.org/10.3390/ijms21197389 |
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author | Alekseev, Aleksandr Cherevatenko, Galina Serdakov, Maksim Pobegalov, Georgii Yakimov, Alexander Bakhlanova, Irina Baitin, Dmitry Khodorkovskii, Mikhail |
author_facet | Alekseev, Aleksandr Cherevatenko, Galina Serdakov, Maksim Pobegalov, Georgii Yakimov, Alexander Bakhlanova, Irina Baitin, Dmitry Khodorkovskii, Mikhail |
author_sort | Alekseev, Aleksandr |
collection | PubMed |
description | Deinococcus radiodurans (Dr) has one of the most robust DNA repair systems, which is capable of withstanding extreme doses of ionizing radiation and other sources of DNA damage. DrRecA, a central enzyme of recombinational DNA repair, is essential for extreme radioresistance. In the presence of ATP, DrRecA forms nucleoprotein filaments on DNA, similar to other bacterial RecA and eukaryotic DNA strand exchange proteins. However, DrRecA catalyzes DNA strand exchange in a unique reverse pathway. Here, we study the dynamics of DrRecA filaments formed on individual molecules of duplex and single-stranded DNA, and we follow conformational transitions triggered by ATP hydrolysis. Our results reveal that ATP hydrolysis promotes rapid DrRecA dissociation from duplex DNA, whereas on single-stranded DNA, DrRecA filaments interconvert between stretched and compressed conformations, which is a behavior shared by E. coli RecA and human Rad51. This indicates a high conservation of conformational switching in nucleoprotein filaments and suggests that additional factors might contribute to an inverse pathway of DrRecA strand exchange. |
format | Online Article Text |
id | pubmed-7583915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-75839152020-10-29 Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA Alekseev, Aleksandr Cherevatenko, Galina Serdakov, Maksim Pobegalov, Georgii Yakimov, Alexander Bakhlanova, Irina Baitin, Dmitry Khodorkovskii, Mikhail Int J Mol Sci Article Deinococcus radiodurans (Dr) has one of the most robust DNA repair systems, which is capable of withstanding extreme doses of ionizing radiation and other sources of DNA damage. DrRecA, a central enzyme of recombinational DNA repair, is essential for extreme radioresistance. In the presence of ATP, DrRecA forms nucleoprotein filaments on DNA, similar to other bacterial RecA and eukaryotic DNA strand exchange proteins. However, DrRecA catalyzes DNA strand exchange in a unique reverse pathway. Here, we study the dynamics of DrRecA filaments formed on individual molecules of duplex and single-stranded DNA, and we follow conformational transitions triggered by ATP hydrolysis. Our results reveal that ATP hydrolysis promotes rapid DrRecA dissociation from duplex DNA, whereas on single-stranded DNA, DrRecA filaments interconvert between stretched and compressed conformations, which is a behavior shared by E. coli RecA and human Rad51. This indicates a high conservation of conformational switching in nucleoprotein filaments and suggests that additional factors might contribute to an inverse pathway of DrRecA strand exchange. MDPI 2020-10-07 /pmc/articles/PMC7583915/ /pubmed/33036395 http://dx.doi.org/10.3390/ijms21197389 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Alekseev, Aleksandr Cherevatenko, Galina Serdakov, Maksim Pobegalov, Georgii Yakimov, Alexander Bakhlanova, Irina Baitin, Dmitry Khodorkovskii, Mikhail Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title | Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title_full | Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title_fullStr | Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title_full_unstemmed | Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title_short | Single-Molecule Insights into ATP-Dependent Conformational Dynamics of Nucleoprotein Filaments of Deinococcus radiodurans RecA |
title_sort | single-molecule insights into atp-dependent conformational dynamics of nucleoprotein filaments of deinococcus radiodurans reca |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7583915/ https://www.ncbi.nlm.nih.gov/pubmed/33036395 http://dx.doi.org/10.3390/ijms21197389 |
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