Molecular and evolutionary aspects of microbial sensory rhodopsins

Biochim Biophys Acta. 2014 May;1837(5):562-77. doi: 10.1016/j.bbabio.2013.05.005. Epub 2013 Jun 1.

Abstract

Retinal proteins (~rhodopsins) are photochemically reactive membrane-embedded proteins, with seven transmembrane α-helices which bind the chromophore retinal (vitamin A aldehyde). They are widely distributed through all three biological kingdoms, eukarya, bacteria and archaea, indicating the biological significance of the retinal proteins. Light absorption by the retinal proteins triggers a photoisomerization of the chromophore, leading to the biological function, light-energy conversion or light-signal transduction. This article reviews molecular and evolutionary aspects of the light-signal transduction by microbial sensory receptors and their related proteins. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.

Keywords: Membrane protein; Phototaxis; Retinal; Signal transfer.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Archaea / chemistry
  • Archaea / physiology
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism
  • Carotenoids / chemistry*
  • Carotenoids / metabolism
  • Chlorophyta / chemistry
  • Chlorophyta / physiology
  • Cyanobacteria / chemistry
  • Cyanobacteria / physiology
  • Evolution, Molecular*
  • Ion Transport
  • Light
  • Light Signal Transduction
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Proteobacteria / chemistry
  • Proteobacteria / physiology
  • Retinaldehyde / chemistry*
  • Retinaldehyde / metabolism
  • Sensory Rhodopsins / chemistry*
  • Sensory Rhodopsins / metabolism

Substances

  • Archaeal Proteins
  • Sensory Rhodopsins
  • phototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis
  • Carotenoids
  • Retinaldehyde