6XZL

Arabidopsis UV-B photoreceptor UVR8 mutant D96N D107N

Summary for 6XZL

• Entry DOI: 10.2210/pdb6xzl/pdb
• Descriptor: Ultraviolet-B receptor UVR8, GLYCEROL (3 entities in total)
• Functional Keywords: uvb, photoreceptor, plant protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 40413.14

Authors

Lau, K.,Hothorn, M. (deposition date: 2020-02-04, release date: 2021-01-13, Last modification date: 2024-01-24)

Primary citation

Podolec, R.,Lau, K.,Wagnon, T.B.,Hothorn, M.,Ulm, R.
A constitutively monomeric UVR8 photoreceptor confers enhanced UV-B photomorphogenesis.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The plant ultraviolet-B (UV-B) photoreceptor UVR8 plays an important role in UV-B acclimation and survival. UV-B absorption by homodimeric UVR8 induces its monomerization and interaction with the E3 ubiquitin ligase COP1, leading ultimately to gene expression changes. UVR8 is inactivated through redimerization, facilitated by RUP1 and RUP2. Here, we describe a semidominant, hyperactive allele, namely , that harbors a glycine-101 to serine mutation. UVR8 overexpression led to weak constitutive photomorphogenesis and extreme UV-B responsiveness. UVR8 was observed to be predominantly monomeric in vivo and, once activated by UV-B, was not efficiently inactivated. Analysis of a UVR8 crystal structure containing the G101S mutation revealed the distortion of a loop region normally involved in stabilization of the UVR8 homodimer. Plants expressing a UVR8 variant combining G101S with the previously described W285A mutation exhibited robust constitutive photomorphogenesis. This work provides further insight into UVR8 activation and inactivation mechanisms and describes a genetic tool for the manipulation of photomorphogenic responses.

PubMed: 33542100
DOI: 10.1073/pnas.2017284118

Experimental method

X-RAY DIFFRACTION (1.39 Å)