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Interactions and Stabilities of the UV RESISTANCE LOCUS8 (UVR8) protein dimer and its key mutants
University of Gothenburg, Gothenburg, Sweden.
Örebro University, School of Science and Technology. (Biokemi)ORCID iD: 0000-0003-3315-8835
University of Gothenburg, Gothenburg, Sweden.
2013 (English)In: Journal of Chemical Information and Modeling, ISSN 1549-9596, E-ISSN 1549-960X, Vol. 53, no 7, p. 1736-1746Article in journal (Refereed) Published
Abstract [en]

The dimeric UVR8 protein is a 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 monomerisation, 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 was 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.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2013. Vol. 53, no 7, p. 1736-1746
National Category
Theoretical Chemistry Physical Chemistry Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:oru:diva-29389DOI: 10.1021/ci4001822ISI: 000322345400018PubMedID: 23745796Scopus ID: 2-s2.0-84880534992OAI: oai:DiVA.org:oru-29389DiVA, id: diva2:626560
Projects
Plant UV-B photbiology
Funder
Swedish Research Council
Note

Funding agency:

University of Gothenburg 

Available from: 2013-06-09 Created: 2013-06-09 Last updated: 2018-05-18Bibliographically approved

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