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Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer
The Holliday junction (HJ) is a DNA intermediate of homologous recombination, involved in many fundamental physiological processes. RuvB, an ATPase motor protein, drives branch migration of the Holliday junction with a mechanism that had yet to be elucidated. Here we report two cryo-EM structures of...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10272136/ https://www.ncbi.nlm.nih.gov/pubmed/37322069 http://dx.doi.org/10.1038/s41467-023-39250-6 |
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author | Rish, Anthony D. Shen, Zhangfei Chen, Zhenhang Zhang, Nan Zheng, Qingfei Fu, Tian-Min |
author_facet | Rish, Anthony D. Shen, Zhangfei Chen, Zhenhang Zhang, Nan Zheng, Qingfei Fu, Tian-Min |
author_sort | Rish, Anthony D. |
collection | PubMed |
description | The Holliday junction (HJ) is a DNA intermediate of homologous recombination, involved in many fundamental physiological processes. RuvB, an ATPase motor protein, drives branch migration of the Holliday junction with a mechanism that had yet to be elucidated. Here we report two cryo-EM structures of RuvB, providing a comprehensive understanding of HJ branch migration. RuvB assembles into a spiral staircase, ring-like hexamer, encircling dsDNA. Four protomers of RuvB contact the DNA backbone with a translocation step size of 2 nucleotides. The variation of nucleotide-binding states in RuvB supports a sequential model for ATP hydrolysis and nucleotide recycling, which occur at separate, singular positions. RuvB’s asymmetric assembly also explains the 6:4 stoichiometry between the RuvB/RuvA complex, which coordinates HJ migration in bacteria. Taken together, we provide a mechanistic understanding of HJ branch migration facilitated by RuvB, which may be universally shared by prokaryotic and eukaryotic organisms. |
format | Online Article Text |
id | pubmed-10272136 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-102721362023-06-17 Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer Rish, Anthony D. Shen, Zhangfei Chen, Zhenhang Zhang, Nan Zheng, Qingfei Fu, Tian-Min Nat Commun Article The Holliday junction (HJ) is a DNA intermediate of homologous recombination, involved in many fundamental physiological processes. RuvB, an ATPase motor protein, drives branch migration of the Holliday junction with a mechanism that had yet to be elucidated. Here we report two cryo-EM structures of RuvB, providing a comprehensive understanding of HJ branch migration. RuvB assembles into a spiral staircase, ring-like hexamer, encircling dsDNA. Four protomers of RuvB contact the DNA backbone with a translocation step size of 2 nucleotides. The variation of nucleotide-binding states in RuvB supports a sequential model for ATP hydrolysis and nucleotide recycling, which occur at separate, singular positions. RuvB’s asymmetric assembly also explains the 6:4 stoichiometry between the RuvB/RuvA complex, which coordinates HJ migration in bacteria. Taken together, we provide a mechanistic understanding of HJ branch migration facilitated by RuvB, which may be universally shared by prokaryotic and eukaryotic organisms. Nature Publishing Group UK 2023-06-15 /pmc/articles/PMC10272136/ /pubmed/37322069 http://dx.doi.org/10.1038/s41467-023-39250-6 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Rish, Anthony D. Shen, Zhangfei Chen, Zhenhang Zhang, Nan Zheng, Qingfei Fu, Tian-Min Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title | Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title_full | Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title_fullStr | Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title_full_unstemmed | Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title_short | Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer |
title_sort | molecular mechanisms of holliday junction branch migration catalyzed by an asymmetric ruvb hexamer |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10272136/ https://www.ncbi.nlm.nih.gov/pubmed/37322069 http://dx.doi.org/10.1038/s41467-023-39250-6 |
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