Crystal structure of RecR, a member of the RecFOR DNA‐repair pathway, from Pseudomonas aeruginosa PAO1. Issue 4 (12th April 2018)

• Record Type: Journal Article
• Authors: Che, Shiyou; Chen, Yujing; Liang, Yakun; Zhang, Qionglin; Bartlam, Mark
• Is Part Of: Acta crystallographica. Volume 74:Issue 4(2018:Apr.)
• Page Start: 222
• Page End: 230
• Publication Date: 2018-04-12
• Subjects: crystal structure -- homologous recombination -- RecR -- DNA repair -- Pseudomonas aeruginosa; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18003503
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The 2.2 Å resolution crystal structure of the homologous recombination protein RecR from P. aeruginosa PAO1 is reported. The crystal structure shows that dimeric P. aeruginosa RecR forms a ring‐like tetramer architecture via crystal symmetry. Abstract : DNA damage is usually lethal to all organisms. Homologous recombination plays an important role in the DNA damage‐repair process in prokaryotic organisms. Two pathways are responsible for homologous recombination in Pseudomonas aeruginosa : the RecBCD pathway and the RecFOR pathway. RecR is an important regulator in the RecFOR homologous recombination pathway in P. aeruginosa . It forms complexes with RecF and RecO that can facilitate the loading of RecA onto ssDNA in the RecFOR pathway. Here, the crystal structure of RecR from P. aeruginosa PAO1 ( Pa RecR) is reported. Pa RecR crystallizes in space group P 61 22, with two monomers per asymmetric unit. Analytical ultracentrifugation data show that Pa RecR forms a stable dimer, but can exist as a tetramer in solution. The crystal structure shows that dimeric Pa RecR forms a ring‐like tetramer architecture via crystal symmetry. The presence of a ligand in the Walker B motif of one RecR subunit suggests a putative nucleotide‐binding site.