Sensory Rhodopsins

Abstract

Motile organisms sense and respond to extracellular stimuli to survive in the various environments in which they live, by changing their movement to migrate towards more favourable habitats or to avoid more harmful habitats. Light is one of the most important signals that provide critical information to biological systems and therefore many organisms utilise light not only as an energy source but also as a signal. Sensory rhodopsin is a photochemically reactive membrane‐embedded protein consisting of seven transmembrane alpha‐helices, which binds the chromophore retinal (vitamin A aldehyde). Sensory rhodopsin is broadly distributed through all three biological kingdoms, eukarya, bacteria and archaea, indicating the biological significance of their light signal conversion.

Key Concepts:

  • Many organisms can sense and respond to light stimuli.

  • Photoactive retinal proteins play important roles in light signal transduction in various organisms.

  • The transcis photoisomerisation of the retinal chromophore triggers the cyclic photoreaction, leading to structural changes of the protein moiety.

  • Photoactivated sensory rhodopsins regulate the activity of the cognate transducer molecules, which control the motility and morphology of the organisms.

  • Sensory rhodopsins have become a focus of interest in part because of their importance to the general understanding of light signal conversion and because of potential application for the novel technology named ‘optogenetics’, in which retinal proteins are utilised to control biological activity with high temporal and spatial resolutions.

Keywords: light; retinal; signal transduction; membrane protein; colour; isomerisation

Figure 1.

Retinal proteins from microorganisms. (a) Chemical structure of the all‐trans retinal protonated Schiff base. (b) Crystal structures of retinal proteins. BR (PDB code: 1C3W) (Luecke et al., ), ASR (PDB code: 1XIO) (Vogeley et al., ), SRII (PDB code: 1H68) (Royant et al., ) and ChR, also called CSR, (PDB code: 3UG9) (Kato et al., ) are coloured by purple, magenta, orange and yellow, respectively. The retinal chromophore covalently binds to a specific Lys residue located at the middle of the membrane via a protonated Schiff base linkage. CP and EC indicate cytoplasmic and extracellular side, respectively. (c) Illustration of absorption spectra of retinal proteins. Retinal proteins show various colours and exhibit two basic functions: the ion pumping and sensing.

Figure 2.

Phylogenetic tree of sensory rhodopsins and BR. They are widespread in archaea, eubacteria and eukarya. Abbreviations: ASR, Anabaena sensory rhodopsin; CSRB, Chlamydomonas sensory rhodopsin B; CSRA, Chlamydomonas sensory rhodopsin A; NpSRII, Natronomonas pharaonis sensory rhodopsin II; HsSRII, Halobacterium salinarum sensory rhodopsin II; HvSRI, Haloarcula vallismortis sensory rhodopsin I; HsSRI, Halobacterium salinarum sensory rhodopsin I; and SrSRI, Salinibacter ruber sensory rhodopsin I.

Figure 3.

Models for signalling by the three types of sensory rhodopsins. (a) SRII forms a tetrameric 2:2 signalling complex with HtrII in the membrane. The SRII–HtrII complex interacts with an adaptor protein CheW and transfers the light signal to CheY via phosphorylation of a kinase CheA. The phosphorylated CheY controls the rotation direction of the flagellar motor apparatus, resulting in negative phototaxis. (b) ASR performs the transcriptional regulation of phycobilisome proteins in collaboration with a putative transducer protein ASRT. (c) CSR mediates the photoinduced membrane depolarisation, leading to a motility change of the cell.

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Further Reading

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Spudich JL and Jung K‐H (2005) Microbial rhodopsin: phylogenetic and functional diversity. In: Briggs WR and Spudich JL (eds) Handbook of Photosensory Receptors, pp. 1–23. Weinheim, Germany: Wiley‐VCH Verlag.

Spudich JL , Sineshchekov OA and Govorunova EG (2013) Mechanism divergence in microbial rhodopsins. Biochimica et Biophysica Acta. doi: 10.1016/j.bbabio.2013.06.006

Sudo Y (2012) Transport and sensory rhodopsins in microorganisms. In: CRC Handbook of Organic Photochemistry and Photobiology, 3rd edn., pp. 1173–1193. Boca Raton, FL: CRC Press.

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Tsukamoto, Takashi, and Sudo, Yuki(Jan 2014) Sensory Rhodopsins. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0022838]