Constitutively active UVR8 photoreceptor variant in Arabidopsis
Arabidopsis thaliana UV RESISTANCE LOCUS 8 (UVR8) is a UV-B photoreceptor that initiates photomorphogenic responses underlying acclimation and UV-B tolerance in plants. UVR8 is a homodimer in its ground state, and UV-B exposure results in its instantaneous monomerization followed by interaction with...
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Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 110; no. 50; pp. 20326 - 20331 |
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Main Authors: | , , , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
National Academy of Sciences
10-12-2013
NATIONAL ACADEMY OF SCIENCES National Acad Sciences |
Subjects: | |
Online Access: | Get full text |
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Summary: | Arabidopsis thaliana UV RESISTANCE LOCUS 8 (UVR8) is a UV-B photoreceptor that initiates photomorphogenic responses underlying acclimation and UV-B tolerance in plants. UVR8 is a homodimer in its ground state, and UV-B exposure results in its instantaneous monomerization followed by interaction with CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1), a major factor in UV-B signaling. UV-B photoreception by UVR8 is based on intrinsic tryptophan aromatic amino acid residues, with tryptophan-285 as the main chromophore. We generated transgenic plants expressing UVR8 with a single amino acid change of tryptophan-285 to alanine. UVR8 ᵂ²⁸⁵ᴬ appears monomeric and shows UV-B–independent interaction with COP1. Phenotypically, the plants expressing UVR8 ᵂ²⁸⁵ᴬ exhibit constitutive photomorphogenesis associated with constitutive activation of target genes, elevated levels of anthocyanins, and enhanced, acclimation-independent UV-B tolerance. Moreover, we have identified COP1, REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1 and 2 (RUP1 and RUP2), and the SUPPRESSOR OF PHYA-105 (SPA) family as proteins copurifying with UVR8 ᵂ²⁸⁵ᴬ. Whereas COP1, RUP1, and RUP2 are known to directly interact with UVR8, we show that SPA1 interacts with UVR8 indirectly through COP1. We conclude that UVR8 ᵂ²⁸⁵ᴬ is a constitutively active UVR8 photoreceptor variant in Arabidopsis , as is consistent with the crucial importance of monomer formation and COP1 binding for UVR8 activity. |
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Bibliography: | http://dx.doi.org/10.1073/pnas.1314336110 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by George Coupland, Max Planck Institute for Plant Breeding Research, Cologne, Germany, and approved October 31, 2013 (received for review July 29, 2013) 2Present address: Department of Pathology, Cancer Institute, New York University School of Medicine, New York, NY 10016. Author contributions: M.H. and R.U. designed research; M.H., M.B., R.Y., F.A.-O., E.V.D.S., G.P., and J.N. performed research; L.R., K.G., and G.D.J. contributed new reagents/analytic tools; M.H., K.G., G.D.J., and R.U. analyzed data; and M.H. and R.U. wrote the paper. 1Present address: Department of Plant Systems Biology, VIB, B-9052 Ghent, Belgium. |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.1314336110 |