Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1861, Issue 1, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbabio.2019.148092
Keywords
Seven transmembrane protein; Thermal stability; Microbial rhodopsin; Flavobacteria
Categories
Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education [2018R1A6A1A03024940, 2017K2A9A1A01092962, 2010-616-000029]
- Penn State University Faculty Development Grant [02060040Z]
- Collaborative Genome Program of the Korea Institute of Marine Science and Technology Promotion (KIMST) - Ministry of Oceans and Fisheries [20180430]
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Although many microbial rhodopsins have been discovered many of organisms in a variety of habitats, little is known about the property and diversity of rhodopsin in flavobacteria. Recent studies discovered that many proteorhodopsin (PR)-like proteins exist in genomes of flavobacteria. Following the isolation of a flavobacterial rhodopsins (FR) from the flavobacteria IMCC1997 from the East Sea of Korea, we characterized its photochemical features. We confirmed that the FR expression is induced by light in the IMCC1997 cell. Upon receiving light energy in vitro, the proton acceptor (D83) and donor (E94) of the FR translocate protons from intracellular to extracellular regions. Compared with proteorhodopsin (PR), the FR from IMCC 1997 cells is very unstable, which may be explained by their primary sequence differences. The ratio of all trans/13-cis retinal conformation does not influence this stability. To measure the stability of FR, we tested heat endurance at 70 degrees C and found that the heat endurance time of some FR mutants increased. Based upon these results, we found the helix E of this protein to be critical for the unstability of FR.
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