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Nat Commun. 2015 Dec 9;6:10079. doi: 10.1038/ncomms10079.

Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue.

Author information

1
Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York 14853, USA.
2
Biophysikalische Chemie, Institut für Biologie, Humboldt-Universität zu Berlin, Berlin 10115, Germany.
3
National Biomedical Center for Advanced ESR Technology, Cornell University, Ithaca, New York 14853, USA.
4
Fachbereich Physik, Institut für Experimentalphysik, Freie Universität Berlin, Berlin 14195, Germany.
5
Lehrstuhl für Biochemie, Universität Bayreuth, Bayreuth 95400, Germany.

Abstract

Light-oxygen-voltage (LOV) receptors sense blue light through the photochemical generation of a covalent adduct between a flavin-nucleotide chromophore and a strictly conserved cysteine residue. Here we show that, after cysteine removal, the circadian-clock LOV-protein Vivid still undergoes light-induced dimerization and signalling because of flavin photoreduction to the neutral semiquinone (NSQ). Similarly, photoreduction of the engineered LOV histidine kinase YF1 to the NSQ modulates activity and downstream effects on gene expression. Signal transduction in both proteins hence hinges on flavin protonation, which is common to both the cysteinyl adduct and the NSQ. This general mechanism is also conserved by natural cysteine-less, LOV-like regulators that respond to chemical or photoreduction of their flavin cofactors. As LOV proteins can react to light even when devoid of the adduct-forming cysteine, modern LOV photoreceptors may have arisen from ancestral redox-active flavoproteins. The ability to tune LOV reactivity through photoreduction may have important implications for LOV mechanism and optogenetic applications.

PMID:
26648256
PMCID:
PMC4682037
DOI:
10.1038/ncomms10079
[Indexed for MEDLINE]
Free PMC Article

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