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Proline 411 biases the conformation of the intrinsically disordered plant UVR8 photoreceptor C27 domain altering the functional properties of the peptide
Chalmers University of Technology, Gothenburg, Sweden.
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden; School of Science and Technology, Örebro University, Örebro, Sweden.
University of Gothenburg, Gothenburg, Sweden.
Örebro universitet, Institutionen för naturvetenskap och teknik. (Biokemi)ORCID-id: 0000-0003-3315-8835
2019 (engelsk)Inngår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, artikkel-id 818Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

UVR8 (UV RESISTANCE LOCUS 8) is a UV-B photoreceptor responsible for initiating UV-B signalling in plants. UVR8 is a homodimer in its signalling inactive form. Upon absorption of UV radiation, the protein monomerizes into its photoactivated state. In the monomeric form, UVR8 binds the E3 ubiquitin ligase COP1 (CONSTITUTIVELY PHOTOMORPHOGENIC 1), triggering subsequent UV-B-dependent photomorphogenic development in plants. Recent in vivoexperiments have shown that the UVR8 C-terminal region (aa 397-423; UVR8C27) alone is sufficient to regulate the activity of COP1. In this work, CD spectroscopy and NMR experiments showed that the UVR8C27domain was non-structured but gained secondary structure at higher temperatures leading to increased order. Bias-exchange metadynamics simulations were also performed to evaluate the free energy landscape of UVR8C27. An inverted free energy landscape was revealed, with a disordered structure in the global energy minimum. Flanking the global energy minimum, more structured states were found at higher energies. Furthermore, stabilization of the low energy disordered state was attributed to a proline residue, P411, as evident from P411A mutant data. P411 is also a key residue in UVR8 binding to COP1. UVR8C27is therefore structurally competent to function as a molecular switch for interaction of UVR8 with different binding partners since at higher free energies different structural conformations are being induced in this peptide. P411 has a key role for this function.

sted, utgiver, år, opplag, sider
Nature Publishing Group, 2019. Vol. 9, artikkel-id 818
HSV kategori
Forskningsprogram
Biokemi
Identifikatorer
URN: urn:nbn:se:oru:diva-70355DOI: 10.1038/s41598-018-37005-8ISI: 000456826200047PubMedID: 30692548Scopus ID: 2-s2.0-85060606046OAI: oai:DiVA.org:oru-70355DiVA, id: diva2:1266640
Forskningsfinansiär
Swedish Research CouncilCarl Tryggers foundation
Merknad

Funding Agencies:

Faculty of Science at University of Gothenburg

Swedish NMR centre at the University of Gothenburg 

Sven and Lily Lawski foundation for Scientific Research

Tilgjengelig fra: 2018-11-28 Laget: 2018-11-28 Sist oppdatert: 2019-02-13bibliografisk kontrollert

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Proline 411 biases the conformation of the intrinsically disordered plant UVR8 photoreceptor C27 domain altering the functional properties of the peptide(7145 kB)94 nedlastinger
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