5svv | pdb_00005svv
Structure and kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis
Structural highlights
Function[ADO1_ARATH] Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedA LOV (Light, Oxygen, or Voltage) domain containing blue-light photoreceptor ZEITLUPE (ZTL) directs circadian timing by degrading clock proteins in plants. Functions hinge upon allosteric differences coupled to the ZTL photocycle; however, structural and kinetic information was unavailable. Herein, we tune the ZTL photocycle over two orders of magnitude. These variants reveal that ZTL complexes with targets independent of light, but dictates enhanced protein degradation in the dark. In vivo experiments definitively show photocycle kinetics dictate the rate of clock component degradation, thereby impacting circadian period. Structural studies demonstrate that photocycle dependent activation of ZTL depends on an unusual dark-state conformation of ZTL. Crystal structures of ZTL LOV domain confirm delineation of structural and kinetic mechanisms and identify an evolutionarily selected allosteric hinge differentiating modes of PAS/LOV signal transduction. The combined biochemical, genetic and structural studies provide new mechanisms indicating how PAS/LOV proteins integrate environmental variables in complex networks. Kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis.,Pudasaini A, Shim JS, Song YH, Shi H, Kiba T, Somers DE, Imaizumi T, Zoltowski BD Elife. 2017 Feb 28;6. pii: e21646. doi: 10.7554/eLife.21646. PMID:28244872[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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