Key determinants for signaling in the sensory rhodopsin II/transducer complex are different between Halobacterium salinarum and Natronomonas pharaonis

The cell membrane of Halobacterium salinarum contains a retinal-binding photoreceptor, sensory rhodopsin II (HsSRII), coupled with its cognate transducer (HsHtrII), allowing repellent phototaxis behavior for shorter wavelength light. Previous studies on SRII from Natronomonas pharaonis (NpSRII) pointed out the importance of the hydrogen bonding interaction between Thr204(NpSRII) and Tyr174(NpSRII) in signal transfer from SRII to HtrII. Here, we investigated the effect on phototactic function by replacing residues in HsSRII corresponding to Thr204(NpSRII) and Tyr174(NpSRII). Whereas replacement of either residue altered the photocycle kinetics, introduction of any mutations at Ser201(HsSRII) and Tyr171(HsSRII) did not eliminate negative phototaxis function. These observations imply the possibility of the presence of an unidentified molecular mechanism for photophobic signal transduction differing from NpSRII-NpHtrII.

Automated summary

By replacing amino acid residues in the photoreceptor HsSRII and its transducer HsHtrII of Halobacterium salinarum, it was found that the hydrogen bonding interaction between Thr204(NpSRII) and Tyr174(NpSRII) plays an important role in phototactic behavior. However, replacing the corresponding residues Ser201(HsSRII) and Tyr171(HsSRII) did not eliminate negative phototaxis function, suggesting the presence of an unidentified molecular mechanism for photophobic signal transduction different from NpSRII-NpHtrII.