{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rish AD"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["3549"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10272136"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["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 c"],"journal":["Nature communications"],"pubmed_title":["Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer."],"pmcid":["PMC10272136"],"funding_grant_id":["R35 GM147465","P41 GM103310","GM1R35GM147465-01","T32 GM118291","T32 GM144293"],"pubmed_authors":["Shen Z","Chen Z","Rish AD","Zhang N","Zheng Q","Fu TM"],"additional_accession":[]},"is_claimable":false,"name":"Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer.","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 c","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-05-28T12:10:41.718Z","creation":"2025-02-19T00:49:58.673Z"},"accession":"S-EPMC10272136","cross_references":{"pubmed":["37322069"],"doi":["10.1038/s41467-023-39250-6"]}}