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Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales
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dc.contributor.author | Paytubi, Sonia | |
dc.contributor.author | McMahon, Stephen | |
dc.contributor.author | Graham, Shirley | |
dc.contributor.author | Liu, Huanting | |
dc.contributor.author | Botting, Catherine Helen | |
dc.contributor.author | Makarova, Kira S. | |
dc.contributor.author | Kroonin, Eugene V. | |
dc.contributor.author | Naismith, Jim | |
dc.contributor.author | White, Malcolm F | |
dc.date.accessioned | 2011-12-12T16:35:45Z | |
dc.date.available | 2011-12-12T16:35:45Z | |
dc.date.issued | 2012-02-14 | |
dc.identifier | 16016046 | |
dc.identifier | cc2611fa-f3f1-4614-b9e1-41f70f79f619 | |
dc.identifier | 000300489200005 | |
dc.identifier | 84863142936 | |
dc.identifier.citation | Paytubi , S , McMahon , S , Graham , S , Liu , H , Botting , C H , Makarova , K S , Kroonin , E V , Naismith , J & White , M F 2012 , ' Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales ' , Proceedings of the National Academy of Sciences of the United States of America , vol. 109 , no. 7 , pp. E398-E405 . https://doi.org/10.1073/pnas.1113277108 | en |
dc.identifier.issn | 0027-8424 | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/47136093 | |
dc.identifier.uri | https://hdl.handle.net/10023/2108 | |
dc.description.abstract | Single-stranded DNA binding proteins (SSBs) based on the OB-fold are considered ubiquitous in nature and play a central role in many DNA transactions including replication, recombination and repair. We demonstrate that the thermoproteales, a clade of hyperthermophilic crenarchaea, lack a canonical SSB. Instead, they encode a distinct ssDNA-binding protein that we term "ThermoDBP", exemplified by protein Ttx1576 from Thermoproteus tenax. ThermoDBP binds specifically to ssDNA with low sequence specificity. The crystal structure of Ttx1576 reveals a unique fold and mechanism for ssDNA binding, consisting of an extended cleft lined with hydrophobic phenylalanine residues and flanked by basic amino acids. Two ssDNA-binding domains are linked by a coiled-coil leucine zipper. ThermoDBP appears to have displaced the canonical SSB during the diversification of the thermoproteales – a highly unusual example where a “ubiquitous” protein has been lost in evolution. | |
dc.format.extent | 8 | |
dc.format.extent | 2628918 | |
dc.language.iso | eng | |
dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America | en |
dc.subject | QH426 Genetics | en |
dc.subject.lcc | QH426 | en |
dc.title | Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales | en |
dc.type | Journal article | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.identifier.doi | https://doi.org/10.1073/pnas.1113277108 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | BBS/B/14426 | en |
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