Anabaena sensory rhodopsin (ASR) is a microbial rhodopsin in the cyanobacterium
sp. PCC7120, and has been suggested to regulate cell processes in a light-quality-dependent
manner (color-discrimination) through interaction with a water-soluble
transducer protein (Tr). However, light-dependent ASR-Tr interaction changes
have not yet to be demonstrated. We applied the transient grating (TG)
method to investigate protein−protein interaction between ASR with Tr.
The molecular diffusion component of the TG signal upon photostimulation
of ASRAT (ASR with an all-trans retinylidene chromophore) revealed that
Tr dissociates from ASR upon formation of the M-intermediate and rebinds
to ASR during the decay of M; i.e. light induces transient dissociation
of ASR and Tr during the photocycle. Further correlating the dissociation
of the ASR-Tr pair with the M-intermediate, no transient dissociation was
observed after the photoexcitation of the blue-shifted ASR13C (ASR with
13-cis, 15-syn chromophore), which does not produce M. This distinction
between ASRAT and ASR13C, the two isomeric forms in a color-sensitive equilibrium
in ASR, provides a potential mechanism for color-sensitive signaling by
ASR.
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