Displacement of the Canonical Single-stranded DNA-binding Protein in the Thermoproteales

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2011 Nov 23

PMID 22106294

Citations 19

Authors

Sonia Paytubi

Stephen A McMahon

Shirley Graham

Huanting Liu

Catherine H Botting

Kira S Makarova

Eugene V Koonin

James H Naismith

Malcolm F White

Affiliations

Soon will be listed here.

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.

Citing Articles

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