Two photosystems controlling behavioural responses of Halobacterium halobium

Hildebrand, Eilo; Dencher, Norbert A.

doi:10.1038/257046a0

Cited by 191 publications

(109 citation statements)

References 15 publications

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“…Bacteriorhodopsin was further characterized as a light-driven proton pump that converts light into chemical energy by powering the ATP-synthase [s]. A photosensory function was postulated at the same time on the basis of action spectra for the photophobic response of swimming cells [3]. Meanwhile, the existence of three additional retinal proteins, each of which occurring in much lower copy number than bacteriorhodopsin, has been demonstrated.…”

Section: Introductionmentioning

confidence: 99%

The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium

et al. 1991

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Halobacterium halobium swims by rotating its polarly inserted flagellar bundle. The cells are attracted by green‐to‐orange light which they can use for photophosphorylation but flee damaging blue or ultraviolet light. It is generally believed that this kind of ‘colour vision’ is achieved by the combined action of two photoreceptor proteins, sensory rhodopsins‐I and ‐II, that switch in the light the rotational sense of the bundle and in consequence the swimming direction of a cell. By expressing the bacteriorhodopsin gene in a photoreceptor‐negative background we have now demonstrated the existence of a proton‐motive force sensor (protometer) and the function of bacteriorhodopsin as an additional photoreceptor covering the high intensity range. When the bacteriorhodopsin‐generated proton‐motive force drops caused by a sudden decrease in light intensity, the cells respond by reversing their swimming direction. This response does not occur when the proton‐motive force is saturated by respiration or fermentation.

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Section: Introductionmentioning

confidence: 99%

The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium

et al. 1991

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“…Halobactetium halobium responds to changes in light intensity [ 1,2] and to chemical gradients in the surrounding medium [3]. Light detected by photosystern 370 acts as a repellent and light detected by photosystem 565 acts as an attractant [2,4].…”

Section: Introductionmentioning

confidence: 99%

“…Light detected by photosystern 370 acts as a repellent and light detected by photosystem 565 acts as an attractant [2,4]. Chemical attractants are glucose and several amino acids,whereas phenol acts as a repellent [3].…”

Section: Introductionmentioning

confidence: 99%

Methylation of membrane proteins is involved in chemosensory and photosensory behavior of Halobacterium halobium

Schimz

1981

FEBS Letters

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“…SR II is the primary light sensor for the photophobic response of halobacteria (17). It is a member of the growing family of microbial rhodopsins that act as light-driven pumps, sensors, and channels (18).…”

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confidence: 99%

Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy

Jiang

Zaitseva

Schmidt

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

131

163

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Membrane proteins are molecular machines that transport ions, solutes, or information across the cell membrane. Electrophysiological techniques have unraveled many functional aspects of ion channels but suffer from the lack of structural sensitivity. Here, we present spectroelectrochemical data on vibrational changes of membrane proteins derived from a single monolayer. ion transfer ͉ membrane potential ͉ proton translocation ͉ vibrational spectroscopy ͉ sensory rhodopsin

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Two photosystems controlling behavioural responses of Halobacterium halobium

Cited by 191 publications

References 15 publications

The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium

The proton pump bacteriorhodopsin is a photoreceptor for signal transduction in Halobacterium halobium

Methylation of membrane proteins is involved in chemosensory and photosensory behavior of Halobacterium halobium

Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy

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