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Crystal Structure of WHY3 from Arabidopsis thalianaCrystal Structure of WHY3 from Arabidopsis thaliana
Structural highlights
FunctionWHY3_ARATH Single-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In the nucleus, is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Can bind double-stranded DNA in vivo.[1] [2] [3] [4] Publication Abstract from PubMedDNA 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. A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum.,Cappadocia L, Parent JS, Sygusch J, Brisson N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1207-11., doi: 10.1107/S1744309113028698. Epub 2013 Oct 26. PMID:24192350[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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