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dc.contributor.authorMacNeill, Stuart
dc.date.accessioned2021-07-21T11:30:02Z
dc.date.available2021-07-21T11:30:02Z
dc.date.issued2021-07-20
dc.identifier.citationMacNeill , S 2021 , ' Remote homology detection identifies a eukaryotic RPA DBD-C-like DNA binding domain as a conserved feature of archaeal Rpa1-like proteins ' , Frontiers in Molecular Biosciences , vol. 8 , 675229 . https://doi.org/10.3389/fmolb.2021.675229en
dc.identifier.issn2296-889X
dc.identifier.otherPURE: 274764701
dc.identifier.otherPURE UUID: e907e57c-332f-4436-bf78-b79db778d417
dc.identifier.otherORCID: /0000-0002-0555-0007/work/97473145
dc.identifier.otherScopus: 85111906933
dc.identifier.urihttp://hdl.handle.net/10023/23612
dc.descriptionOpen Access publication fees were provided by the University of St Andrews.en
dc.description.abstractThe eukaryotic single-stranded DNA binding factor replication protein A (RPA) is essential for DNA replication, repair and recombination. RPA is a heterotrimer containing six related OB folds and a winged helix-turn-helix (wH) domain. The OB folds are designated DBD-A through DBD-F, with DBD-A through DBD-D being directly involved in ssDNA binding. DBD-C is located at the C-terminus of the RPA1 protein and has a distinctive structure that includes an integral C4 zinc finger, while the wH domain is found at the C-terminus of the RPA2 protein. Previously characterised archaeal RPA proteins fall into a number of classes with varying numbers of OB folds, but one widespread class includes proteins that contain a C4 or C3H zinc finger followed by a 100-120 amino acid C-terminal region reported to lack detectable sequence or structural similarity. Here, the sequences spanning this zinc finger and including the C-terminal region are shown to comprise a previously unrecognised DBD-C-like OB fold, confirming the evolutionary relatedness of this group of archaeal RPA proteins to eukaryotic RPA1. The evolutionary relationship between eukaryotic and archaeal RPA is further underscored by the presence of RPA2-like proteins comprising an OB fold and C-terminal winged helix (wH) domain in multiple species and crucially, suggests that several biochemically characterised archaeal RPA proteins previously thought to exist as monomers are likely to be RPA1-RPA2 heterodimers.
dc.format.extent8
dc.language.isoeng
dc.relation.ispartofFrontiers in Molecular Biosciencesen
dc.rightsCopyright © 2021 MacNeill. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en
dc.subjectRPAen
dc.subjectOB folden
dc.subjectWinged helix domainen
dc.subjectArchaeaen
dc.subjectssDNAen
dc.subjectDNA repairen
dc.subjectDNA replicationen
dc.subjectQH426 Geneticsen
dc.subject3rd-DASen
dc.subject.lccQH426en
dc.titleRemote homology detection identifies a eukaryotic RPA DBD-C-like DNA binding domain as a conserved feature of archaeal Rpa1-like proteinsen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.identifier.doihttps://doi.org/10.3389/fmolb.2021.675229
dc.description.statusPeer revieweden


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