UVR8
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Through Protein, Plant and Flowering plant
Evolution
Although the complete genome sequence is only available from a limited number of angiosperms, bioinformatic analysis suggests that there are a large number of UVR8 orthologs. Both number and position of key residues seem to be well conserved among angiosperms but also other plant species (e.g., Chlamydomonas reinhardtii and Volvox carteri). The latter implies that UVR8 potentially appeared before the evolutionary split in vascular land plants which would be rational considering that at that time the amount of UV-B radiation that penetrated the earth surface was higher as the ozone layer was not fully developed, hence UV protection and acclimation would be of crucial importance.
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Structure
UVR8 is a β-propeller protein with 7 blade-shaped β-sheets. It shares sequence homology with mammalian proteins involved in regulating chromatin condensation, for example the human RCC1 gene product. In the dark state, UVR8 forms a homodimer that is localized in the cytosol, but UV-B illumination induces the dissociation of UVR8 dimer to its respective monomers and translocation to the nucleus occurs. The dimer is held together via a complex salt bridge network.
Mechanism
Upon UV-B irradiation, light is absorbed by one or more Trp residues which are situated adjacent to Arg residues which form salt bridges across the dimer interface. It is thought that this light absorption induces the disruption of the salt-bridges and thus leads to the molecule's monomerization. Following monomerization, UVR8 accumulates in the nucleus where it interacts with a protein called constitutively photomorphogenic 1 (COP1). COP1 is known to act as an E3 Ubiquitin ligase that targets key transcription factors for ubiquitination and proteasome-mediated degradation. However, in the case of UVR8, it has been shown to act as a positive regulator of UVR8-mediated UV-B signalling. Upon UV-B illumination, UVR8 interacts via a C-terminal 27 amino acid region with the WD40 domain of COP1 in the nucleus, which triggers the induction of ELONGATED HYPOCOTYL 5 (HY5) — a key transcription factor for several UV-B responsive genes, and overall results in UV-B acclimation.
External links[1]
- "Detailed picture of a UV-sensing protein". Scripps Research Institute. 9 February 2012.
- Sunhats for plants QUite Interesting PDB Structure article at PDBe