Structural highlightsFunctionWHY3_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]
References
- ↑ Xiong JY, Lai CX, Qu Z, Yang XY, Qin XH, Liu GQ. Recruitment of AtWHY1 and AtWHY3 by a distal element upstream of the kinesin gene AtKP1 to mediate transcriptional repression. Plant Mol Biol. 2009 Nov;71(4-5):437-49. doi: 10.1007/s11103-009-9533-7. Epub, 2009 Aug 11. PMID:19669906 doi:http://dx.doi.org/10.1007/s11103-009-9533-7
- ↑ Marechal A, Parent JS, Veronneau-Lafortune F, Joyeux A, Lang BF, Brisson N. Whirly proteins maintain plastid genome stability in Arabidopsis. Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14693-8. doi:, 10.1073/pnas.0901710106. Epub 2009 Aug 7. PMID:19666500 doi:http://dx.doi.org/10.1073/pnas.0901710106
- ↑ Cappadocia L, Marechal A, Parent JS, Lepage E, Sygusch J, Brisson N. Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair. Plant Cell. 2010 Jun;22(6):1849-67. Epub 2010 Jun 15. PMID:20551348 doi:10.1105/tpc.109.071399
- ↑ Cappadocia L, Parent JS, Zampini E, Lepage E, Sygusch J, Brisson N. A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage. Nucleic Acids Res. 2011 Sep 12. PMID:21911368 doi:10.1093/nar/gkr740
| |