A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum
A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum
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DOI：
10.1107/s1744309113028698
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发表时间：
2013-11-01
影响因子：
0.9
通讯作者：
Brisson, Normand
中科院分区：
文献类型：
--
作者：
Cappadocia, Laurent;Parent, Jean-Sebastien;Brisson, Normand
DNA双链断裂是基因组中经常出现的高度有害的基因组损伤。为了保护其遗传信息的完整性，所有生物都进化出了专门的DNA修复机制。Whirly蛋白通过以非序列特异性方式结合单链DNA来调节植物叶绿体和线粒体中的DNA修复。虽然大多数表明Whirly蛋白参与DNA修复的结果已经在拟南芥中获得，但迄今为止仅报道了马铃薯Whirly蛋白WHY 1和WHY 2的晶体结构。本文报道了A. thaliana（WHY 1、WHY 2和WHY 3）的研究表明，这些结构相似的蛋白质组装成四聚体。此外，与马铃薯WHY 2-DNA复合物的结构比对显示，这些蛋白质中的残基被正确定向以非序列特异性方式结合单链DNA。
DNA double-strand breaks are highly detrimental genomic lesions that routinely arise in genomes. To protect the integrity of their genetic information, all organisms have evolved specialized DNA-repair mechanisms. Whirly proteins modulate DNA repair in plant chloroplasts and mitochondria by binding single-stranded DNA in a non-sequence-specific manner. Although most of the results showing the involvement of the Whirly proteins in DNA repair have been obtained in Arabidopsis thaliana, only the crystal structures of the potato Whirly proteins WHY1 and WHY2 have been reported to date. The present report of the crystal structures of the three Whirly proteins from A. thaliana (WHY1, WHY2 and WHY3) reveals that these structurally similar proteins assemble into tetramers. Furthermore, structural alignment with a potato WHY2-DNA complex reveals that the residues in these proteins are properly oriented to bind single-stranded DNA in a non-sequence-specific manner.