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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Koonin, Eugene V. Botting, Catherine H. White, Malcolm F. Paytubi, Sonia Liu, Huanting Makarova, Kira S. Mcmahon, Stephen A. Graham, Shirley Naismith, James H. |
| Description | Author Affiliation: Paytubi S ( Biomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, United Kingdom.); |
| Abstract | ssDNA-binding proteins (SSBs) based on the oligonucleotide-binding 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 the protein Ttx1576 from Thermoproteus tenax. ThermoDBP binds specifically to ssDNA with low sequence specificity. The crystal structure of Ttx1576 reveals a unique fold and a 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 of the loss of a 'ubiquitous' protein during evolution. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 7 |
| Volume Number | 109 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2012-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA-Binding Proteins Metabolism Thermoproteales Cloning, Molecular Crystallography, X-Ray Chemistry Genetics Protein Binding Protein Folding Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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