Displacement of the Canonical Single-Stranded DNA-Binding Protein in the Thermoproteales
Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales Sonia Paytubia,1,2, Stephen A. McMahona,2, Shirley Grahama, Huanting Liua, Catherine H. Bottinga, Kira S. Makarovab, Eugene V. Kooninb, James H. Naismitha,3, and Malcolm F. Whitea,3 aBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, United Kingdom; and bNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894 AUTHOR SUMMARY Proteins are the major structural and biochemical route involved direct puri- operational components of cells. Even fication and identification of proteins the simplest organisms possess hundreds thatcouldbindtossDNAinoneofthe of different proteins, and more complex Thermoproteales, Thermoproteus tenax. organisms typically have many thou- This approach resulted in the identifi- sands. Because all living beings, from cation of the product of the gene ttx1576 microbes to humans, are related by as a candidate for the missing SSB. evolution, they share a core set of pro- We proceeded to characterize the teins in common. Proteins perform properties of the Ttx1576 protein, (which fundamental roles in key metabolic we renamed “ThermoDBP” for Ther- processes and in the processing of in- moproteales DNA-binding protein), formation from DNA via RNA to pro- showing that it has all the biochemical teins. A notable example is the ssDNA- properties consistent with a role as a binding protein, SSB, which is essential functional SSB, including a clear prefer- for DNA replication and repair and is ence for ssDNA binding and low se- widely considered to be one of the quence specificity. Using crystallographic few core universal proteins shared by analysis, we solved the structure of the alllifeforms.Herewedemonstrate Fig.
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