Structural basis of ultraviolet-B perception by UVR8.

Abstract:

:The Arabidopsis thaliana protein UVR8 is a photoreceptor for ultraviolet-B. Upon ultraviolet-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, which triggers a signalling pathway for ultraviolet protection. The mechanism by which UVR8 senses ultraviolet-B remains largely unknown. Here we report the crystal structure of UVR8 at 1.8 Å resolution, revealing a symmetric homodimer of seven-bladed β-propeller that is devoid of any external cofactor as the chromophore. Arginine residues that stabilize the homodimeric interface, principally Arg 286 and Arg 338, make elaborate intramolecular cation-π interactions with surrounding tryptophan amino acids. Two of these tryptophans, Trp 285 and Trp 233, collectively serve as the ultraviolet-B chromophore. Our structural and biochemical analyses identify the molecular mechanism for UVR8-mediated ultraviolet-B perception, in which ultraviolet-B radiation results in destabilization of the intramolecular cation-π interactions, causing disruption of the critical intermolecular hydrogen bonds mediated by Arg 286 and Arg 338 and subsequent dissociation of the UVR8 homodimer.

journal_name

Nature

journal_title

Nature

authors

Wu D,Hu Q,Yan Z,Chen W,Yan C,Huang X,Zhang J,Yang P,Deng H,Wang J,Deng X,Shi Y

doi

10.1038/nature10931

subject

Has Abstract

pub_date

2012-02-29 00:00:00

pages

214-9

issue

7393

eissn

0028-0836

issn

1476-4687

pii

nature10931

journal_volume

484

pub_type

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