Localization and dimer stability of a newly identified microbial rhodopsin from a polar, non-motile green algae.
OBJECTIVE
The eukaryotic plasma membrane localized light-gated proton-pumping rhodopsins possesses great optogenetic applications for repolarization (silencing) of the neuronal activity simply by light illumination. Very few plasma membrane localized proton-pumping rhodopsins of a eukaryotic origin are known that have optogenetic potential. Our objective was to identify and characterize microbial rhodopsin of an eukaryotic origin that expresses on plasma membrane. The plasma membrane localized light-gated proton pump of an eukaryotic origin hold great promise to be used as an optogenetic tools for the neurobiology.


RESULTS
Here, we had characterized the cellular expression and membrane localization of a new rhodopsin in Antarctican algae Coccomyxa subellipsoidea. It is the first algal ion pumping rhodopsin that localizes to the plasma membrane of the eukaryotic cells. Coccomyxa subellipsoidea rhodopsin exists in the monomeric and dimeric state both the in vivo and in vitro. The dimeric form of the Coccomyxa subellipsoidea rhodopsin is resistant to heat and detergent denaturants.
['Ranjan|Peeyush|P|', 'Kateriya|Suneel|S|http://orcid.org/0000-0001-5428-4297']
D020418:Algal Proteins D000595:Amino Acid Sequence D000864:Antarctic Regions D002462:Cell Membrane D000460:Chlorophyta D015151:Immunoblotting D008027:Light D055503:Protein Multimerization D055550:Protein Stability D017494:Proton Pumps D012243:Rhodopsin D017386:Sequence Homology, Amino Acid
Proton-pumping rhodopsin Optogenetics Coccomyxa subellipsoidea Chlorella vulgaris Localization of the microbial rhodopsin in eukaryotes