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

Ulrike Scheib, Matthias Broser, Oana M. Constantin, Shang Yang, Shiqiang Gao, Shatanik Mukherjee, Katja Stehfest, Georg Nagel, Christine E. Gee () and Peter Hegemann ()
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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

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04428-w

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