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'''Unreleased structure'''
{{STRUCTURE_4koo|  PDB=4koo  |  SCENE=  }}
===Crystal Structure of WHY1 from Arabidopsis thaliana===


The entry 4koo is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/WHY1_ARATH WHY1_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 nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.<ref>PMID:14960277</ref> <ref>PMID:17217467</ref> <ref>PMID:19669906</ref> <ref>PMID:19666500</ref> <ref>PMID:20551348</ref> <ref>PMID:21911368</ref>  


Authors: Cappadocia, L., Parent, J.S., Brisson, N., Sygusch, J.
==About this Structure==
[[4koo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KOO OCA].  


Description: Crystal Structure of WHY1 from Arabidopsis thaliana
==Reference==
<references group="xtra"/><references/>
[[Category: Brisson, N.]]
[[Category: Cappadocia, L.]]
[[Category: Parent, J S.]]
[[Category: Sygusch, J.]]
[[Category: Dna binding protein]]
[[Category: Plant]]
[[Category: Single-stranded dna binding protein]]
[[Category: Whirly]]

Revision as of 08:29, 13 November 2013

Template:STRUCTURE 4koo

Crystal Structure of WHY1 from Arabidopsis thaliana

Function

[WHY1_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 nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.[1] [2] [3] [4] [5] [6]

About this Structure

4koo is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Desveaux D, Subramaniam R, Despres C, Mess JN, Levesque C, Fobert PR, Dangl JL, Brisson N. A "Whirly" transcription factor is required for salicylic acid-dependent disease resistance in Arabidopsis. Dev Cell. 2004 Feb;6(2):229-40. PMID:14960277
  2. ↑ Yoo HH, Kwon C, Lee MM, Chung IK. Single-stranded DNA binding factor AtWHY1 modulates telomere length homeostasis in Arabidopsis. Plant J. 2007 Feb;49(3):442-51. Epub 2007 Jan 1. PMID:17217467 doi:https://dx.doi.org/10.1111/j.1365-313X.2006.02974.x
  3. ↑ 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:https://dx.doi.org/10.1007/s11103-009-9533-7
  4. ↑ 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:https://dx.doi.org/10.1073/pnas.0901710106
  5. ↑ 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
  6. ↑ 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

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