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Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding
Author(s) -
Timmins Joanna,
Leiros Ingar,
McSweeney Sean
Publication year - 2007
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601760
Subject(s) - biology , dna , genetics , dna binding protein , computational biology , transcription factor , gene
The crystal structure of the complex formed between Deinococcus radiodurans RecR and RecO (drRecOR) has been determined. In accordance with previous biochemical characterisation, the drRecOR complex displays a RecR:RecO molecular ratio of 2:1. The biologically relevant drRecOR entity consists of a heterohexamer in the form of two drRecO molecules positioned on either side of the tetrameric ring of drRecR, with their OB (oligonucleotide/oligosaccharide‐binding) domains pointing towards the interior of the ring. Mutagenesis studies validated the protein–protein interactions observed in the crystal structure and allowed mapping of the residues in the drRecOR complex required for DNA binding. Furthermore, the preferred DNA substrate of drRecOR was identified as being 3′‐overhanging DNA, as encountered at ssDNA–dsDNA junctions. Together these results suggest a possible mechanism for drRecOR recognition of stalled replication forks.