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Rhodopsin(s) in eubacteria.

W D Hoff1, H C Matthijs, H Schubert

  • 1Department of Microbiology, E.C. Slater Institute, BioCentrum, University of Amsterdam, Nieuwe Achtergracht 127, 1018 WS Amsterdam, Netherlands.

Biophysical Chemistry
|September 1, 1995
PubMed
Summary
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Researchers identified novel eubacterial photoreceptors, revealing that the photoactive yellow protein (PYP) uses a non-retinal chromophore, while a rhodopsin mediates complementary chromatic adaptation in cyanobacteria.

Area of Science:

  • Microbiology
  • Photobiology
  • Biochemistry

Background:

  • Photosensory signal transduction in Eubacteria is poorly understood, unlike well-characterized photosynthetic mechanisms.
  • Eubacterial rhodopsin-like proteins are emerging as key photoreceptors.

Purpose of the Study:

  • To investigate novel eubacterial photosensory proteins and their chromophores.
  • To elucidate the molecular mechanisms of photosensory signal transduction in Eubacteria.

Main Methods:

  • Crystallographic and photochemical analyses of the photoactive yellow protein (PYP).
  • Biochemical assays and genetic manipulations to study complementary chromatic adaptation in cyanobacteria.
  • Inhibition and restoration experiments using nicotine and retinal.

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Main Results:

  • The PYP chromophore was definitively shown to be different from retinal, despite photochemical similarities to rhodopsins.
  • Complementary chromatic adaptation in Calothrix sp. was dependent on retinal biosynthesis and mediated by a rhodopsin.
  • These findings present the first eubacterial photoreceptors amenable to molecular study.

Conclusions:

  • Eubacteria utilize diverse photoreceptor systems beyond bacteriochlorophyll and bacteriorhodopsin.
  • PYP represents a novel class of photoreceptor with a non-retinal chromophore.
  • Rhodopsins play a significant role in eubacterial light-mediated responses like chromatic adaptation.