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


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 ? =?31?ms and decays with ? =?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.

SUBMITTER: Scheib U 

PROVIDER: S-EPMC5967339 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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

Scheib Ulrike U   Broser Matthias M   Constantin Oana M OM   Yang Shang S   Gao Shiqiang S   Mukherjee Shatanik S   Stehfest Katja K   Nagel Georg G   Gee Christine E CE   Hegemann Peter P  

Nature communications 20180524 1


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  ...[more]

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