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Interactions and Stabilities of the UV RESISTANCE LOCUS8 (UVR8) Protein Dimer and Its Key Mutants

Journal article
Authors Min Wu
Åke Strid
Leif A Eriksson
Published in Journal of Chemical Information and Modeling
Volume 53
Issue 7
Pages 1736-1746
ISSN 1549-9596
Publication year 2013
Published at Department of Chemistry and Molecular Biology
Pages 1736-1746
Language en
Links dx.doi.org/10.1021/ci4001822
Keywords UVR8 dimer; MD simulations; Mutations; Umbrella sampling; Monomerisation
Subject categories Biophysical chemistry, Theoretical Chemistry, Biochemistry

Abstract

The dimeric UVR8 protein is an ultraviolet-B radiation (280−315 nm) photoreceptor responsible for the first step in UV−B regulation of gene expression in plants. Its action comprises the actual absorption of the UV quanta by a tryptophan array at the protein−protein interface, followed by monomerization and subsequent aggregation with downstream signaling components. A crystal structure of the Arabidopsis thaliana tryptophan-rich wild type UVR8 protein dimer was recently published, showing the presence of several salt bridges involving arginines R146, R286, R338, and R354. In this work, molecular dynamics simulations in conjunction with umbrella sampling were used to calculate the binding free energy for the wild type UVR8 dimer and three of its mutants (R286A, R338A, and R286A/R338A), in order to verify whether the key mutants are able to disrupt the dimeric structure as indicated experimentally.

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