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

Author

Listed:
  • Estella F. Yee

    (Baker Laboratory, Cornell University)

  • Ralph P. Diensthuber

    (Biophysikalische Chemie, Institut für Biologie, Humboldt-Universität zu Berlin)

  • Anand T. Vaidya

    (Baker Laboratory, Cornell University
    Present address: Division of Biology, California Institute of Technology, Pasadena, California 91125, USA.)

  • Peter P. Borbat

    (Baker Laboratory, Cornell University
    National Biomedical Center for Advanced ESR Technology, Cornell University)

  • Christopher Engelhard

    (Fachbereich Physik, Institut für Experimentalphysik, Freie Universität Berlin)

  • Jack H. Freed

    (Baker Laboratory, Cornell University
    National Biomedical Center for Advanced ESR Technology, Cornell University)

  • Robert Bittl

    (Fachbereich Physik, Institut für Experimentalphysik, Freie Universität Berlin)

  • Andreas Möglich

    (Biophysikalische Chemie, Institut für Biologie, Humboldt-Universität zu Berlin
    Lehrstuhl für Biochemie, Universität Bayreuth)

  • Brian R. Crane

    (Baker Laboratory, Cornell University)

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.

Suggested Citation

  • Estella F. Yee & Ralph P. Diensthuber & Anand T. Vaidya & Peter P. Borbat & Christopher Engelhard & Jack H. Freed & Robert Bittl & Andreas Möglich & Brian R. Crane, 2015. "Signal transduction in light–oxygen–voltage receptors lacking the adduct-forming cysteine residue," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10079
    DOI: 10.1038/ncomms10079
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    Cited by:

    1. Stefanie S. M. Meier & Elina Multamäki & Américo T. Ranzani & Heikki Takala & Andreas Möglich, 2024. "Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Julia Dietler & Renate Gelfert & Jennifer Kaiser & Veniamin Borin & Christian Renzl & Sebastian Pilsl & Américo Tavares Ranzani & Andrés García de Fuentes & Tobias Gleichmann & Ralph P. Diensthuber & , 2022. "Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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