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A novel structure of DNA repair protein RecO from Deinococcus radiodurans

机译:放射球菌DNA修复蛋白RecO的新结构

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摘要

Recovery of arrested replication requires coordinated action of DNA repair, replication, and recombination machineries. Bacterial RecO protein is a member of RecF recombination repair pathway important for replication recovery. RecO possesses two distinct activities in vitro, closely resembling those of eukaryotic protein Rad52: DNA annealing and RecA-mediated DNA recombination. Here we present the crystal structure of the RecO protein from the extremely radiation resistant bacteria Deinococcus radiodurans (DrRecO) and characterize its DNA binding and strand annealing properties. The RecO structure is totally different from the Rad52 structure. DrRecO is comprised of three structural domains: an N-terminal domain which adopts an OB-fold, a novel a-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the multidomain architecture is conserved between RecO proteins from other bacterial species and is suitable to elucidate sites of protein-protein and DNA-protein interactions necessary for RecO functions during the replication recovery and DNA repair.
机译:恢复被阻止的复制需要DNA修复,复制和重组机制的协同作用。细菌RecO蛋白是RecF重组修复途径的成员,对复制恢复很重要。 RecO在体外具有两种不同的活性,与真核蛋白Rad52的活性非常相似:DNA退火和RecA介导的DNA重组。在这里,我们介绍了来自极耐辐射细菌Deinococcus radiodurans(DrRecO)的RecO蛋白的晶体结构,并表征了其DNA结合和链退火特性。 RecO结构与Rad52结构完全不同。 DrRecO由三个结构域组成:采用OB折叠的N端结构域,新颖的a螺旋结构域和不寻常的锌结合结构域。序列比对表明,多域结构在其他细菌的RecO蛋白之间是保守的,适合于阐明在复制恢复和DNA修复过程中RecO功能所需的蛋白质-蛋白质和DNA-蛋白质相互作用的位点。

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