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Please use this identifier to cite or link to this item: http://hdl.handle.net/10023/2108
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Title: Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales
Authors: Paytubi, Sonia
McMahon, Stephen
Graham, Shirley
Liu, Huanting
Botting, Catherine Helen
Makarova, Kira S.
Kroonin, Eugene V.
Naismith, Jim
White, Malcolm F
Keywords: QH426 Genetics
Issue Date: 14-Feb-2012
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 .
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.
Version: Postprint
Status: Peer reviewed
URI: http://hdl.handle.net/10023/2108
DOI: http://dx.doi.org/10.1073/pnas.1113277108
ISSN: 0027-8424
Type: Journal article
Rights: This is the accepted version of this article (c) the authors. The published version is available at DOI: 10.1073/pnas.1113277108
Appears in Collections:University of St Andrews Research
Biology Research
Chemistry Research
Biomedical Sciences Research Complex (BSRC) Research



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