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dc.contributor.authorJolly, Samson M.
dc.contributor.authorZhang, Han
dc.contributor.authorStrittmatter, Lara
dc.contributor.authorHendricks, Gregory M.
dc.contributor.authorDhabaria, Avantika
dc.contributor.authorUeberheide, Beatrix
dc.contributor.authorZamore, Phillip D.
dc.date2022-08-11T08:08:24.000
dc.date.accessioned2022-08-23T15:53:50Z
dc.date.available2022-08-23T15:53:50Z
dc.date.issued2019-12-09
dc.date.submitted2020-01-27
dc.identifier.citation<p>bioRxiv 869172; doi: https://doi.org/10.1101/869172. <a href="https://doi.org/10.1101/869172" target="_blank">Link to preprint on bioRxiv service.</a></p>
dc.identifier.doi10.1101/869172
dc.identifier.urihttp://hdl.handle.net/20.500.14038/29431
dc.description.abstractArgonaute proteins use nucleic acid guides to protect organisms against transposons and viruses. In the eubacterium Thermus thermophilus, the DNA-guided Argonaute TtAgo defends against transformation by DNA plasmids. Here, we report that TtAgo also participates in DNA replication. TtAgo binds small DNA guides derived from the chromosomal region where replication terminates and associates with proteins known to act in DNA replication. T. thermophilus deploys a single type II topoisomerase, gyrase. When gyrase is inhibited, T. thermophilus relies on TtAgo to complete replication of its circular genome; loss of both gyrase and TtAgo activity produces long filaments that fail to separate into individual bacteria. We propose that the primary role of TtAgo is to help T. thermophilus disentangle the catenated circular chromosomes made by DNA replication.
dc.language.isoen_US
dc.relationNow published in Cell doi: 10.1016/j.cell.2020.07.036
dc.rightsThe copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC-ND 4.0 International license.
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectMicrobiology
dc.subjectArgonaute Protein
dc.subjectDNA Replication
dc.subjectThermus thermophilus
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectMicrobiology
dc.subjectNucleic Acids, Nucleotides, and Nucleosides
dc.titleA DNA-guided Argonaute Protein Functions in DNA Replication in Thermus thermophilus [preprint]
dc.typePreprint
dc.source.journaltitlebioRxiv
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2668&amp;context=faculty_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/1658
dc.identifier.contextkey16347416
refterms.dateFOA2022-08-23T15:53:50Z
html.description.abstract<p>Argonaute proteins use nucleic acid guides to protect organisms against transposons and viruses. In the eubacterium <em>Thermus thermophilus</em>, the DNA-guided Argonaute TtAgo defends against transformation by DNA plasmids. Here, we report that TtAgo also participates in DNA replication. TtAgo binds small DNA guides derived from the chromosomal region where replication terminates and associates with proteins known to act in DNA replication. <em>T. thermophilus</em> deploys a single type II topoisomerase, gyrase. When gyrase is inhibited, <em>T. thermophilus</em> relies on TtAgo to complete replication of its circular genome; loss of both gyrase and TtAgo activity produces long filaments that fail to separate into individual bacteria. We propose that the primary role of TtAgo is to help <em>T. thermophilus</em> disentangle the catenated circular chromosomes made by DNA replication.</p>
dc.identifier.submissionpathfaculty_pubs/1658
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.contributor.departmentDepartment of Radiology
dc.contributor.departmentRNA Therapeutics Institute
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology


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The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC-ND 4.0 International license.
Except where otherwise noted, this item's license is described as The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It is made available under a CC-BY-NC-ND 4.0 International license.