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At least 739 records · Page 41Linked to original sources
PubMed1994

Sensory rhodopsin I photocycle intermediate SRI380 contains 13-cis retinal bound via an unprotonated Schiff base.

Sensory rhodopsin I (SRI), the mutated derivative SRI-D76N and the complex of SRI with its transducer HtrI were overexpressed in Halobacterium salinarium and analyzed by resonance Raman spectroscopy. In the initial state SRI contains all-trans retinal bound via a protonated Schiff base as confirmed by retinal extraction which yields 95 +/- 3% all-trans retinal. The photocycle intermediate absorbing maximally at 380 nm (SRI380) contains a Schiff base linkage between the protein and 13-cis retinal. Extraction of illuminated SRI yields up to 93% 13-cis retinal. Neither the mutation D76N nor HtrI changed the vibrational pattern of the chromophore.

Bacteriorhodopsins↗
PubMed1994

Phototactic behaviour of the archaebacterial Natronobacterium pharaonis.

Natronobacterium pharaonis can react tactically to photo- and chemostimuli. It moves by rotation of a flagellar bundle which is monopolarly inserted. Under sufficient oxygen supply the photophobic response of N. pharaonis has been measured. The resulting action spectrum matches the absorption spectrum of the purified retinylidene protein psR-II. Retical synthesis could be inhibited by nicotine. Cells grown in the presence of nicotine show a strongly reduced photoresponse, which could be restored by addition of retinal. These data identify psR-II as the receptor for negative phototaxis.

Chemotaxis↗
PubMed1995

Reason for the lack of light-dark adaptation in pharaonis phoborhodopsin: reconstitution with 13-cis-retinal.

The reconstitution of pharaonis phoborhodopsin was performed by incubation of its opsin with 13-cis-retinal. Spectrum change was very slow, and two phases of the change were observed: the first and second phases are due to the transient formation of 13-cis pigment and spontaneous isomerization to all-trans-retinal, respectively. Slow binding supports an idea that the retinal binding pocket of ppR is highly restricted. Being bent in the configuration, 13-cis-retinal cannot be accommodated in the pocket due to the steric hindrance. This is a possible reason for the lack of light-dark adaptation.

Archaeal Proteins↗
PubMed1995

Functional expression of bacteriorhodopsin in oocytes allows direct measurement of voltage dependence of light induced H+ pumping.

We report on the first successful expression of the light driven H+ pump, bacteriorhodopsin, into the plasma membrane of oocytes from Xenopus laevis. The light induced photocurrents which reflect the pumping of H+ by BR were analysed under voltage clamp conditions. At least 100 active BR molecules per microns 2 were expressed in the plasma membrane so that both the voltage clamp and giant patch clamp method could be applied. We show that H+ pumping by BR is modulated by the membrane potential, i.e. the pump current shows strong voltage dependence in the range measured between -165 mV to +60 mV.

Animals↗
PubMed1996

Immunolocalization of X-arrestin in human cone photoreceptors.

X-arrestin is a recently identified retina-specific gene of unknown function. Affinity-purified anti-peptide antibody to human X-arrestin was prepared, and used in Western blot analysis of human retinal proteins and for immunohistochemistry on human retinal sections. By Western blot analysis, the antibody specifically bound to an approximately 47 kDa protein, and by indirect immunofluorescence specifically labeled cone photoreceptors with greatest intensity in their outer segments. In single and double label experiments, the localization of X-arrestin immunoreactivity was compared with immunolabeling patterns obtained with antibodies to red/green cone opsin, rhodopsin, and S-antigen. The results showed that X-arrestin is expressed in red-, green- and blue-sensitive cones in the human retina.

Amino Acid Sequence↗
PubMed1996

High-performance liquid chromatographic analysis of retinal and retinol isomers.

Normal-phase chromatograms of retinal- and retinol isomers using various mobile phrases are presented, showing that in n-hexane--tert.-butyl methyl ether and also in n-heptane--tert.-butyl methyl ether the elution order for retinol is 13-cis-, 11-cis-, 9-cis- and all trans-retinol, whereas in n-hexane-1,4-dioxane 11-cis- elutes before 13-cis-retinol. Assignment of these main retinal and retinol peaks was performed using pure crystals of isomers, measurement of absorbance spectra and analysis of NMR spectra. The new mobile phase n-heptane-tert.-butyl methyl ether allows best baseline separation of the commonly occurring isomeric forms in reasonably short analysis time. In addition, eight di-cis- and tri-cis-retinol isomers were tentatively identified. The chromatograms show that former identifications in the literature are inconsistent or wrong.

Chromatography, High Pressure Liquid↗
PubMed1987

Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process.

Possible steps in the folding of bacteriorhodopsin are revealed by studying the refolding and interaction of two fragments of the molecule reconstituted in lipid vesicles. (1) Two denatured bacteriorhodopsin fragments have been purified starting from chymotryptically cleaved bacteriorhodopsin. Cleaved bacteriorhodopsin has been renatured from a mixture of the fragments in Halobacterium lipids/retinal/dodecyl sulfate solution following removal of dodecyl sulfate by precipitation with potassium. The renatured molecules have the same absorption spectrum and extinction coefficient as native cleaved bacteriorhodopsin. They are integrated into small lipid vesicles as a mixture of monomers and aggregates. Extended lattices form during the partial dehydration process used to orient samples for X-ray and neutron crystallography. (2) Correct refolding of cleaved bacterioopsin occurs upon renaturation in the absence of retinal. Regeneration of the chromophore and reformation of the purple membrane lattice are observed following subsequent addition of all-trans retinal. (3) The two chymotryptic fragments have been reinserted separately into lipid vesicles and refolded in the absence of retinal. Circular dichroism spectra of the polypeptide backbone transitions indicate that they have regained a highly alpha-helical structure. The kinetics of chromophore regeneration following reassociation have been studied by absorption spectroscopy. Upon vesicle fusion, the refolded fragments first reassociate, then bind retinal and finally regenerate cleaved bacteriorhodopsin. The complex formed in the absence of retinal is kinetically indistinguishable from cleaved bacterioopsin. The refolded fragments in lipid vesicles are stable for months, both as separate entities and after reassociation. These observations provide further evidence that the native folded structure of bacteriorhodopsin lies at a free energy minimum. They are interpreted in terms of a two-stage folding mechanism for membrane proteins in which stable transmembrane helices are first formed. They subsequently pack without major rearrangement to produce the tertiary structure.

Bacteriorhodopsins↗
PubMed1989

The transverse location of the retinal chromophore in the purple membrane by diffusion-enhanced energy transfer.

We have used fluorescence energy transfer in the rapid-diffusion limit (RDL) to estimate the trans-membrane depth of retinal in the purple membrane (PM). Chelates of Tb(III) are excellent energy donors for the retinal chromophore of PM, having a maximum Ro value for Förster energy transfer of approximately 62 A (assuming a donor quantum yield of 1). Energy transfer rates were measured from the time-resolved emission kinetics of the donor. The distance of closest approach between chelates and the chromophore was estimated by simulating RDL energy-transfer rate constants according to geometric models of either PM sheets or membrane vesicles. The apparent rate constant for RDL energy transfer between Tb(III)HED3A and retinal in PM sheets is 1.5(+/- 0.1) x 10(6) M-1 s-1, corresponding to a depth of approximately 10 +/- 2 A for the retinal chromophore. Cell envelope vesicles (CEVs) from Halobacterium halobium were studied by using RDL energy transfer to assess the proximity of retinal to either the extracellular or intracellular face of the PM. The estimated depth of retinal from the extravesicular face of the PM is 10 +/- 3 A, based on the RDL energy-transfer rate constant. Energy-transfer levels to retinal in the PM were estimated by an indirect method with energy donors trapped in the inner-aqueous space of CEVs. The rate constants derived for this arrangement are too low to be consistent with the shortest depth of retinal deduced for PM sheets. Thus, the intravesticular face of CEVs, corresponding to the cytoplasmic face of cells, is the more distant surface from the chromophore of bacteriorhodopsin.

Bacteriorhodopsins↗
PubMed1995

Expression and localization of inhibin alpha-subunit in rat retinal photoreceptor cells.

To determine whether rat retinal photoreceptor cells produce inhibin, a molecule closely related to activin, a multifunctional growth factor in the transforming growth factor beta superfamily (TGF beta), we have conducted immunohistochemistry using specific antibodies for inhibin which were raised against a synthetic N-terminal fragment of the alpha-subunit of inhibin. The mature inhibin molecule was identified at both the inner and outer segments of photoreceptor cells. To determine if messenger RNA for the alpha-subunit of inhibin is expressed in the retinal cells, both in situ hybridization with a specific probe and the reverse transcription-polymerase chain reaction (RT-PCR) technique with primers specific for the alpha-subunit of inhibin were used. Messenger RNA expression of the alpha-subunit of inhibin was detected by RT-PCR and localized in the photoreceptor cells as determined by in situ hybridization. In addition, the identity of the cDNA product of RT-PCR was verified with Southern analysis and DNA sequencing. The localization of mature inhibin protein and its corresponding message to photoreceptor cells suggest that inhibin may have a paracrine function in the retina, perhaps in the photoreceptor cells themselves.

Animals↗
PubMed1989

Spatial distribution of the inhibitory effect of peripheral non-informative cues on simple reaction time to non-fixated visual targets.

It is known that reaction time (RT) for the detection of a light target at extrafoveal locations is lengthened by a previous non-informative light cue at the same location. We describe an additional inhibitory effect from cues remote from the target but occurring within the same lateral or altitudinal visual hemifield. Subjects made a speeded key-press response to the second of two successive light flashes in a pair while maintaining fixation. Each of the two flashes could appear at random in one of four positions, two in the right and two in the left visual fields, or two in the upper and two in the lower visual fields. We found an RT prolongation not only for cued over uncued positions, but also for within-field non-coincident cue-target pairs over between-fields cue-target pairs. The within-field inhibitory effect, though smaller than the same-location effect, was fully apparent even when the target occurred at 1 degree of visual angle from the midline and at 29 degrees from the cue. Both effects were seen with cue-target asynchronies ranging from 0.2 to 1.5 sec. The results are relevant to the understanding of the neural mechanisms for covert shifts of attention across the main meridians of the visual field.

Adult↗