Crystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans
- 17 February 2005
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 24 (5), 906-918
- https://doi.org/10.1038/sj.emboj.7600582
Abstract
The RecFOR pathway has been shown to be essential for DNA repair through the process of homologous recombination in bacteria and, recently, to be important in the recovery of stalled replication forks following UV irradiation. RecO, along with RecR, RecF, RecQ and RecJ, is a principal actor in this fundamental DNA repair pathway. Here we present the three‐dimensional structure of a member of the RecO family. The crystal structure of Deinococcus radiodurans RecO (drRecO) reveals possible binding sites for DNA and for the RecO‐binding proteins within its three discrete structural regions: an N‐terminal oligonucleotide/oligosaccharide‐binding domain, a helical bundle and a zinc‐finger motif. Furthermore, drRecO was found to form a stable complex with RecR and to bind both single‐ and double‐stranded DNA. Mutational analysis confirmed the existence of multiple DNA‐binding sites within the protein.Keywords
This publication has 38 references indexed in Scilit:
- BRCA2 Function in DNA Binding and Recombination from a BRCA2-DSS1-ssDNA StructureScience, 2002
- Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coatNature, 2002
- Genome of the Extremely Radiation-Resistant Bacterium Deinococcus radiodurans Viewed from the Perspective of Comparative GenomicsMicrobiology and Molecular Biology Reviews, 2001
- The effect of ionic conditions on the conformations of supercoiled DNA. II. equilibrium catenationJournal of Molecular Biology, 1997
- The effect of ionic conditions on the conformations of supercoiled DNA. I. sedimentation analysisJournal of Molecular Biology, 1997
- Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNANature, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Purification and Characterization of the Escherichia coli RecO Protein: Renaturation of Complementary Single-stranded DNA Molecules Catalyzed by the RecO ProteinJournal of Molecular Biology, 1994
- Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constantsJournal of Applied Crystallography, 1993
- Protein Structure Comparison by Alignment of Distance MatricesJournal of Molecular Biology, 1993