Cyclic nucleotides (e.g. cAMP and cGMP) are ubiquitous second messengers which affect various cellular functions. Photoactivated adenylyl cyclase (PAC) and guanylyl cyclase rhodopsin (Rh-GC) increase the concentrations of cyclic nucleotides upon illumination, serving as promising second-generation tools in optogenetics. We here report on a novel enzyme rhodopsin (Rh-PDE) which was found in the choanoflagellate Salpingoeca rosetta and contains a C-terminal cyclic nucleotide phosphodiesterase (PDE) domain. Rh-PDE exhibited the hydrolysis activity toward both cAMP and cAMP in a light-dependent manner. Thus, Rh-PDE may hold promise as a potential optogenetic tool for light control of intracellular cyclic nucleotides, for example, to study cyclic nucleotide–associated signal transduction cascades.
Research Area “Optical control of biological functions for the elucidation of biological systems”
Research Theme “Attempts to vision restortion by applying enzyme rhodopsins”
Kazuho Yoshida, Satoshi P. Tsunoda, Leonid S. Brown and Hideki Kandori. “A unique choanoflagellate enzyme rhodopsin with cyclic nucleotide phosphodiesterase activity”. The Journal of Biological Chemistry, Published online March 16, 2017, doi: 10.1074/jbc.M117.775569.
Satoshi Tsunoda, Ph.D. visiting associate professor
Department of Life Science and Applied Chemistry, Nagoya Institute of Technology
Life Innovation Group, Department of Innovation Research, JST