Complex oligomeric structure of a truncated form of DdrA: a protein required for the extreme radiotolerance of Deinococcus

Biochimica Et Biophysica Acta
Irina GutscheLaurence Serre

Abstract

In order to preserve their genome integrity, organisms have developed elaborate tactics for genome protection and repair. The Deinococcus radiodurans bacteria famous for their extraordinary tolerance toward high doses of radiations or long period of desiccation, possess some specific genes with unknown function which are related to their survival in such extreme conditions. Among them, ddrA is an orphan gene specific of Deinococcus genomes. DdrA, the product of this gene was suggested to be a component of the DNA end protection system. Here we provide a three-dimensional reconstruction of the Deinococcus deserti DdrA((1-160)) by electron microscopy. Although not functional in vivo, this truncated protein keeps its DNA binding ability at the wild-type level. DdrA((1-160)) has a complex three-dimensional structure based on a heptameric ring that can self-associate to form a larger molecular weight assembly. We suggest that the complex architecture of DdrA plays a role in the substrate specificity and favors an efficient DNA repair.

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Citations

Jun 12, 2009·The Journal of Biological Chemistry·Cédric A NoraisMichael M Cox
Dec 9, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Mitsugu YamadaIssay Narumi
Mar 5, 2011·Microbiology and Molecular Biology Reviews : MMBR·Dea Slade, Miroslav Radman
Jan 20, 2009·Journal of Molecular Biology·Andreja Vujicić-ZagarLaurence Serre
Aug 26, 2009·Molecular Microbiology·Rémi DulermoArjan De Groot
Feb 27, 2009·Extremophiles : Life Under Extreme Conditions·Hirofumi OhbaIssay Narumi
Nov 3, 2020·Computational and Structural Biotechnology Journal·Zijing ChenYe Zhao
May 31, 2021·Extremophiles : Life Under Extreme Conditions·Claire Bouthier de la TourFabrice Confalonieri

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