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Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli
Interactions between proteins and single-stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination. Thus, understanding detailed mechanisms of these interactions is necessary to uncover regulatory rules occurring in all living cel...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cambridge University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10392684/ https://www.ncbi.nlm.nih.gov/pubmed/37529279 http://dx.doi.org/10.1017/qrd.2022.15 |
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author | Kubiak, Krzysztof Wien, Frank Yadav, Indresh Jones, Nykola C. Vrønning Hoffmann, Søren Le Cam, Eric Cossa, Antoine Geinguenaud, Frederic van der Maarel, Johan R. C. Węgrzyn, Grzegorz Arluison, Véronique |
author_facet | Kubiak, Krzysztof Wien, Frank Yadav, Indresh Jones, Nykola C. Vrønning Hoffmann, Søren Le Cam, Eric Cossa, Antoine Geinguenaud, Frederic van der Maarel, Johan R. C. Węgrzyn, Grzegorz Arluison, Véronique |
author_sort | Kubiak, Krzysztof |
collection | PubMed |
description | Interactions between proteins and single-stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination. Thus, understanding detailed mechanisms of these interactions is necessary to uncover regulatory rules occurring in all living cells. The RNA-binding Hfq is a pleiotropic bacterial regulator that mediates many aspects of nucleic acid metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small regulatory RNA as cofactors. In addition, Hfq helps to compact double-stranded DNA. In this paper, we focused on the action of Hfq on ssDNA. A combination of experimental methodologies, including spectroscopy and molecular imaging, has been used to probe the interactions of Hfq and its amyloid C-terminal region with ssDNA. Our analysis revealed that Hfq binds to ssDNA. Moreover, we demonstrate for the first time that Hfq drastically changes the structure and helical parameters of ssDNA, mainly due to its C-terminal amyloid-like domain. The formation of the nucleoprotein complexes between Hfq and ssDNA unveils important implications for DNA replication and recombination. |
format | Online Article Text |
id | pubmed-10392684 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Cambridge University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-103926842023-08-01 Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli Kubiak, Krzysztof Wien, Frank Yadav, Indresh Jones, Nykola C. Vrønning Hoffmann, Søren Le Cam, Eric Cossa, Antoine Geinguenaud, Frederic van der Maarel, Johan R. C. Węgrzyn, Grzegorz Arluison, Véronique QRB Discov Research Article Interactions between proteins and single-stranded DNA (ssDNA) are crucial for many fundamental biological processes, including DNA replication and genetic recombination. Thus, understanding detailed mechanisms of these interactions is necessary to uncover regulatory rules occurring in all living cells. The RNA-binding Hfq is a pleiotropic bacterial regulator that mediates many aspects of nucleic acid metabolism. The protein notably mediates mRNA stability and translation efficiency by using stress-related small regulatory RNA as cofactors. In addition, Hfq helps to compact double-stranded DNA. In this paper, we focused on the action of Hfq on ssDNA. A combination of experimental methodologies, including spectroscopy and molecular imaging, has been used to probe the interactions of Hfq and its amyloid C-terminal region with ssDNA. Our analysis revealed that Hfq binds to ssDNA. Moreover, we demonstrate for the first time that Hfq drastically changes the structure and helical parameters of ssDNA, mainly due to its C-terminal amyloid-like domain. The formation of the nucleoprotein complexes between Hfq and ssDNA unveils important implications for DNA replication and recombination. Cambridge University Press 2022-09-07 /pmc/articles/PMC10392684/ /pubmed/37529279 http://dx.doi.org/10.1017/qrd.2022.15 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/This is an Open Access article, distributed under the terms of the Creative Commons Attribution licence (http://creativecommons.org/licenses/by/4.0), which permits unrestricted re-use, distribution and reproduction, provided the original article is properly cited. |
spellingShingle | Research Article Kubiak, Krzysztof Wien, Frank Yadav, Indresh Jones, Nykola C. Vrønning Hoffmann, Søren Le Cam, Eric Cossa, Antoine Geinguenaud, Frederic van der Maarel, Johan R. C. Węgrzyn, Grzegorz Arluison, Véronique Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title | Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title_full | Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title_fullStr | Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title_full_unstemmed | Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title_short | Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli |
title_sort | amyloid-like hfq interaction with single-stranded dna: involvement in recombination and replication in escherichia coli |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10392684/ https://www.ncbi.nlm.nih.gov/pubmed/37529279 http://dx.doi.org/10.1017/qrd.2022.15 |
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