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The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders
During the initiation step of bacterial genome replication, replicative helicases depend on specialized proteins for their loading onto oriC. DnaC and DnaI were the first loaders to be characterized. However, most bacteria do not contain any of these genes, which are domesticated phage elements that...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9912922/ https://www.ncbi.nlm.nih.gov/pubmed/36762863 http://dx.doi.org/10.1107/S2059798323000281 |
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author | Cargemel, Claire Marsin, Stéphanie Noiray, Magali Legrand, Pierre Bounoua, Halil Li de la Sierra-Gallay, Inès Walbott, Hélène Quevillon-Cheruel, Sophie |
author_facet | Cargemel, Claire Marsin, Stéphanie Noiray, Magali Legrand, Pierre Bounoua, Halil Li de la Sierra-Gallay, Inès Walbott, Hélène Quevillon-Cheruel, Sophie |
author_sort | Cargemel, Claire |
collection | PubMed |
description | During the initiation step of bacterial genome replication, replicative helicases depend on specialized proteins for their loading onto oriC. DnaC and DnaI were the first loaders to be characterized. However, most bacteria do not contain any of these genes, which are domesticated phage elements that have replaced the ancestral and unrelated loader gene dciA several times during evolution. To understand how DciA assists the loading of DnaB, the crystal structure of the complex from Vibrio cholerae was determined, in which two VcDciA molecules interact with a dimer of VcDnaB without changing its canonical structure. The data showed that the VcDciA binding site on VcDnaB is the conserved module formed by the linker helix LH of one monomer and the determinant helix DH of the second monomer. Interestingly, DnaC from Escherichia coli also targets this module onto EcDnaB. Thanks to their common target site, it was shown that VcDciA and EcDnaC could be functionally interchanged in vitro despite sharing no structural similarity. This represents a milestone in understanding the mechanism employed by phage helicase loaders to hijack bacterial replicative helicases during evolution. |
format | Online Article Text |
id | pubmed-9912922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-99129222023-02-14 The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders Cargemel, Claire Marsin, Stéphanie Noiray, Magali Legrand, Pierre Bounoua, Halil Li de la Sierra-Gallay, Inès Walbott, Hélène Quevillon-Cheruel, Sophie Acta Crystallogr D Struct Biol Research Papers During the initiation step of bacterial genome replication, replicative helicases depend on specialized proteins for their loading onto oriC. DnaC and DnaI were the first loaders to be characterized. However, most bacteria do not contain any of these genes, which are domesticated phage elements that have replaced the ancestral and unrelated loader gene dciA several times during evolution. To understand how DciA assists the loading of DnaB, the crystal structure of the complex from Vibrio cholerae was determined, in which two VcDciA molecules interact with a dimer of VcDnaB without changing its canonical structure. The data showed that the VcDciA binding site on VcDnaB is the conserved module formed by the linker helix LH of one monomer and the determinant helix DH of the second monomer. Interestingly, DnaC from Escherichia coli also targets this module onto EcDnaB. Thanks to their common target site, it was shown that VcDciA and EcDnaC could be functionally interchanged in vitro despite sharing no structural similarity. This represents a milestone in understanding the mechanism employed by phage helicase loaders to hijack bacterial replicative helicases during evolution. International Union of Crystallography 2023-02-06 /pmc/articles/PMC9912922/ /pubmed/36762863 http://dx.doi.org/10.1107/S2059798323000281 Text en © Claire Cargemel et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Papers Cargemel, Claire Marsin, Stéphanie Noiray, Magali Legrand, Pierre Bounoua, Halil Li de la Sierra-Gallay, Inès Walbott, Hélène Quevillon-Cheruel, Sophie The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title | The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title_full | The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title_fullStr | The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title_full_unstemmed | The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title_short | The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders |
title_sort | lh–dh module of bacterial replicative helicases is the common binding site for dcia and other helicase loaders |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9912922/ https://www.ncbi.nlm.nih.gov/pubmed/36762863 http://dx.doi.org/10.1107/S2059798323000281 |
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