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Bacteriorhodopsin (bR) is a light-driven proton pump that uses the energy of a photon to pump protons across the cell membrane. It is found in many halophilic archaea, but not in eukaryotes. Therefore, bR has been widely used for a molecular indicator of salt stress in halophilic archaea. In this study, we investigated the function of bR as a salt stress indicator from the viewpoint of the protein structural stability. The functional stability was tested by using two different methods, the salt tolerance test and the fluorescence intensity recovery after photobleaching (FRAP). In the salt tolerance test, we confirmed that the salt-adapted strain of Halobacillus halophilus (H. halophilus) is more tolerant to salt stress than the salt-sensitive strain of Halorubrum sodomense (H. sodomense). However, the salt-induced change in the fluorescence intensity of bR in H. halophilus was lower than that in H. sodomense. The salt treatment to the cells showed no significant difference between these two strains. These results imply that the change in the bR fluorescence intensity in the two strains was not comparable. We examined the salt tolerance of H. halophilus using an indicator protein, halorhodopsin (hR). The salt tolerance test showed that hR does not change its fluorescence intensity in H. halophilus under salt stress, indicating that the protein functional stability of hR is not affected by salt stress. In contrast, the salt stress did not change the fluorescence intensity of bR in H. sodomense. This result suggests that the functional stability of bR was reduced by salt stress. Furthermore, we studied the salt tolerance of bR in vivo using a bR-deficient mutant of H. halophilus, which confirmed the in vivo salt tolerance of bR. These results suggest that the salt tolerance of H. halophilus bR can be examined using the salt tolerance test and FRAP. In addition, this method is useful for observing the salt tolerance of other halophilic proteins. © 2018 IOP Publishing Ltd.
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