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Photochemical reaction mechanism of UV-B-induced monomerization of UVR8 dimers as the first signaling event in UV-B-regulated gene expression in plants
Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.
Örebro University, School of Science and Technology. (Biokemi)ORCID iD: 0000-0003-3315-8835
Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg, Sweden.
2014 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 118, p. 951-965Article in journal (Refereed) Published
Abstract [en]

The Arabidopsis thaliana UV RESISTANCE LOCUS8 (UVR8) protein has been identified to specifically mediate photomorphogenic UV-B responses by acting as a UV-B photoreceptor. The dimeric structure of the UVR8 protein dissociates into signaling–active monomers upon UV-B exposure, and the monomers rapidly interact with downstream signaling components to regulate gene expression. UVR8 monomers revert to dimers in the absence of UV-B radiation, thereby reversing transcription activation. UVR8 amino acid residues W233 and W285 have been identified to play critical roles in the UVR8 dimer for the response to UV-B irradiation. In the present work, the photo-reaction mechanism for UVR8 monomerization is explored using quantum chemical cluster calculations, and evaluated by molecular dynamics simulations using the wild type UVR8 dimer and novel force field parameters developed for intermediate radicals formed in the photochemical process. Three different models are investigated, which show that the preferred mechanism for UVR8 monomerization involves electron transfer from residue W233 to W285 and onwards to R338 initiated by UV-B irradiation, coupled to simultaneous proton transfer from W233 to D129 leading to the formation of protonated D129, a deprotonated W233 radical and a neutral R338 radical.. Due to the formation of the neutral R338 radical, salt bridges involving this residue are disrupted together with the concomitant interruption of several other key salt bridges R286-D96, R286-D107, R338-D44, R354-E43 and R354-E53. The resulting large decrease in protein-protein interaction energy arising from this sequence of events lead to the monomerization of the UVR8 dimer. The mechanism presented is in accord with all experimental data available to date.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2014. Vol. 118, p. 951-965
Keywords [en]
Amino acid residues; Arabidopsis thaliana; Force field parameters; Molecular dynamics simulations; Photochemical process; Protein-protein interactions; Sequence of events; Signaling components
National Category
Physical Chemistry Biochemistry and Molecular Biology
Research subject
Physical Chemistry; Biochemistry
Identifiers
URN: urn:nbn:se:oru:diva-33022DOI: 10.1021/jp4104118ISI: 000330610400011PubMedID: 24410443Scopus ID: 2-s2.0-84893504425OAI: oai:DiVA.org:oru-33022DiVA, id: diva2:686312
Projects
ULTRAVIOLET RADIATION AS AN ENVIRONMENTAL STIMULI IN BIOLOGICAL SYSTEMS: PERCEPTION, SIGNALLING, MOLECULAR RESPONSES AND MORPHOGENESIS
Funder
Swedish Research CouncilCarl Tryggers foundation
Note

Funding Agency:

Faculty of Science at the University of Gothenburg

Available from: 2014-01-11 Created: 2014-01-11 Last updated: 2017-10-18Bibliographically approved

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Strid, ÅkeEriksson, Leif A

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