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Theoretical prediction of the protein-protein interaction between Arabidopsis thaliana COP1 and UVR8

Journal article
Authors Min Wu
Åke Strid
Leif A Eriksson
Published in Theoretical Chemistry accounts
Volume 132
Pages 1371-1382
ISSN 1432-881X
Publication year 2013
Published at Department of Chemistry and Molecular Biology
Pages 1371-1382
Language en
Links dx.doi.org/10.1007/s00214-013-1371-...
Keywords Arabidopsis thaliana COP1 Docking Modeling Mutation Protein–protein interaction UVR8 WD40
Subject categories Biophysical chemistry, Theoretical Chemistry, Biochemistry and Molecular Biology

Abstract

In plants, ultraviolet-B radiation (280–315 nm) regulates gene expression and plant morphology through the UV RESPONSE LOCUS 8 (UVR8) photoreceptor. The first signaling event after quantal absorbance is the interaction of the UVR8 C-terminus with the E3 ubiquitin ligase CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1). The nature of the interaction between these two proteins is hitherto unknown. A protein homology model of the Arabidopsis thaliana COP1 seven-bladed propeller WD40 repeat domain and de novo folds of the C-terminal 27 amino acid (amino acids 397–423) peptide of Arabidopsis UVR8 (UVR8397−423) is herein reported. Using a theoretical computational docking protocol, the interaction between COP1 and UVR8 was predicted. A core motif was identified in UVR8397−423 comprising adjacent hydrophobic residues V410 and P411 together with a charged residue D412, homologous to corresponding motifs in other COP1-binding proteins, such as ELONGATED HYPOCOTYL 5 (HY5), cryptochrome 1 (CRY1), and salt tolerance proteins STO/STH. The protein–protein interaction between the COP1 WD40 repeat domain and UVR8397−423 reveals binding within a region of COP1 overlapping with the binding site for HY5 and the other COP1-interacting proteins. This study provides a framework for understanding docking between UVR8 and COP1, which in turn gives clues for experimental testing of UVR8/COP1 interaction.

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