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Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

Author

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  • Ulrike Scheib

    (Humboldt-Universität zu Berlin)

  • Matthias Broser

    (Humboldt-Universität zu Berlin)

  • Oana M. Constantin

    (University Medical Center Hamburg-Eppendorf)

  • Shang Yang

    (Julius-Maximilians-University of Würzburg)

  • Shiqiang Gao

    (Julius-Maximilians-University of Würzburg)

  • Shatanik Mukherjee

    (Humboldt-Universität zu Berlin)

  • Katja Stehfest

    (Humboldt-Universität zu Berlin)

  • Georg Nagel

    (Julius-Maximilians-University of Würzburg)

  • Christine E. Gee

    (University Medical Center Hamburg-Eppendorf)

  • Peter Hegemann

    (Humboldt-Universität zu Berlin)

Abstract

The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio >1000. After light excitation the putative signaling state forms with τ = 31 ms and decays with τ = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 Å) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.

Suggested Citation

  • Ulrike Scheib & Matthias Broser & Oana M. Constantin & Shang Yang & Shiqiang Gao & Shatanik Mukherjee & Katja Stehfest & Georg Nagel & Christine E. Gee & Peter Hegemann, 2018. "Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04428-w
    DOI: 10.1038/s41467-018-04428-w
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