TY  - INPR
A1  - Lamm, Gerrit H. U.
A1  - Marin, Egor
A1  - Alekseev, Alexey
A1  - Schellbach, Anna V.
A1  - Stetsenko, Artem
A1  - Bourenkov, Gleb
A1  - Borshchevskiy, Valentin
A1  - Asido, Marvin
A1  - Agthe, Michael
A1  - Engilberge, Sylvain
A1  - Rose, Samuel L.
A1  - Caramello, Nicolas
A1  - Royant, Antoine
A1  - Schneider, Thomas R.
A1  - Bateman, Alex
A1  - Mager, Thomas
A1  - Moser, Tobias
A1  - Wachtveitl, Josef
A1  - Guskov, Albert
A1  - Kovalev, Kirill
T1  - CryoRhodopsins: a comprehensive characterization of a group of microbial rhodopsins from cold environments
T2  - bioRxiv
N2  - Microbial rhodopsins are omnipresent on Earth, however the vast majority of them remain uncharacterized. Here we describe a new rhodopsin group from cold-adapted organisms and cold environments, such as glaciers, denoted as CryoRhodopsins (CryoRs). Our data suggest that CryoRs have dual functionality switching between inward transmembrane proton translocation and photosensory activity, both of which can be modulated with UV light. CryoR1 exhibits two subpopulations in the ground state, which upon light activation lead to transient photocurrents of opposing polarities. A distinguishing feature of the group is the presence of a buried arginine residue close to the cytoplasmic face of its members. Combining single-particle cryo-electron microscopy and X-ray crystallography with the rhodopsin activation by lit, we demonstrate that the arginine stabilizes a UV-absorbing intermediate of an extremely slow CryoRhodopsin photocycle. Together with extensive spectroscopic characterization, our investigations on CryoR1 and CryoR2 proteins reveal mechanisms of photoswitching in the newly identified group and demonstrate principles of the adaptation of these rhodopsins to low temperatures.Microbial rhodopsins are omnipresent on Earth, however the vast majority of them remain uncharacterized. Here we describe a new rhodopsin group from cold-adapted organisms and cold environments, such as glaciers, denoted as CryoRhodopsins (CryoRs). Our data suggest that CryoRs have dual functionality switching between inward transmembrane proton translocation and photosensory activity, both of which can be modulated with UV light. CryoR1 exhibits two subpopulations in the ground state, which upon light activation lead to transient photocurrents of opposing polarities. A distinguishing feature of the group is the presence of a buried arginine residue close to the cytoplasmic face of its members. Combining single-particle cryo-electron microscopy and X-ray crystallography with the rhodopsin activation by light, we demonstrate that the arginine stabilizes a UV-absorbing intermediate of an extremely slow CryoRhodopsin photocycle. Together with extensive spectroscopic characterization, our investigations on CryoR1 and CryoR2 proteins reveal mechanisms of photoswitching in the newly identified group and demonstrate principles of the adaptation of these rhodopsins to low temperatures.
Y1  - 2024
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/83787
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-837870
UR  - https://www.biorxiv.org/content/10.1101/2024.01.15.575777v2
IS  - 2024.01.15.575777 Version 2
PB  - bioRxiv
ER  -