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At least 505 records · Page 28Linked to original sources
PubMed1995

Effects of upstream deletions on light- and oxygen-regulated bacterio-opsin gene expression in Halobacterium halobium.

The bacterio-opsin gene (bop) of Halobacterium halobium is located within a cluster with three other genes. Growth conditions of high light intensity and low oxygen tension induce bop gene cluster expression. To identify putative regulatory factor binding sites upstream of the bop gene, we have compared sequences upstream of the bop gene with the corresponding sequences from two other genes in the bop gene cluster. Conserved sequence motifs were observed which may mediate the effect of high light intensity and/or low oxygen tension on bop gene expression. Based on these motifs, a set of mutants was constructed which contained deletions upstream of the bop gene. These constructs were tested in a host strain where bop gene expression is independent of oxygen regulation and in another strain where it is regulated by oxygen and light. The minimal upstream sequence required for both light- and oxygen-regulated bop gene expression was determined to be 54 bp.

Bacteriorhodopsins↗
PubMed1988

Transcription of genes involved in bacterio-opsin gene expression in mutants of a halophilic archaebacterium.

Recent studies on the regulation of the bacterio-opsin (bop) gene of the archaebacterium Halobacterium halobium suggest that the brp and putative bat genes are involved in bop gene expression or purple membrane assembly. These two genes are located 526 and 1,602 base pairs, respectively, upstream of the bop gene and are both transcribed in the opposite orientation to the bop gene. Transcription of the bop, brp, and putative bat genes was characterized in the wild type, 11 Bop mutants, and a Bop revertant by using a series of RNA probes. Quantitation of the relative mRNA levels for these three genes in the wild type revealed that the brp and bat transcripts are present at approximately 2 and 4%, respectively, of bop mRNA levels under the growth conditions used. Northern (RNA) blot analysis of Bop mutants indicated that insertions in the brp gene affect expression of the putative bat gene. In addition, deletion of most of the bat gene resulted in virtually undetectable levels of bop and brp mRNAs. These and other results lead us to propose that (i) brp gene expression can affect bat gene expression and (ii) the putative bat gene is involved in activating bop and brp gene expression.

Bacteriorhodopsins↗
PubMed1993

Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.

The genes coding for bacterioopsin, haloopsin, and sensory opsin I of a halobacterial isolate from the Red Sea called Halobacterium sp. strain SG1 have been cloned and sequenced. The deduced protein sequences were aligned to the previously known halobacterial retinal proteins. The addition of these new sequences lowered the number of conserved residues to only 23 amino acids, or 8% of the alignment. Data base searches with two highly conserved peptides as well as with an alignment profile yielded no significant similarity to any other protein, so the halobacterial retinal proteins should be regarded as a distinct protein family. The protein alignment was used to make predictions about the structure of the retinal proteins as well as about the amino acids in contact with retinal proteins. These results were in excellent agreement with the structural model of bacteriorhodopsin of Halobacterium halobium as well as with mutant studies, indicating that (i) structure predictions based on the sequences of a membrane protein family can be quite accurate; (ii) halorhodopsin and sensory rhodopsin I have tertiary structures similar to that of bacteriorhodopsin; (iii) conserved amino acids do not take part in reactions specific for one group of proteins, e.g., proton translocation for bacteriorhodopsins, but have a crucial role in determining the conformation and reactions of the chromophore; and (iv) the general mode of action (light-induced chromophore and protein movements) is the same for all halobacterial retinal proteins, ion pumps as well as sensors.

Amino Acid Sequence↗
PubMed2006

Heterogeneity in regeneration of bacteriorhodopsin from bacterio-opsin and all-trans retinal at high temperatures: implications for dynamic structural fluctuations.

Measurements of regeneration kinetics were performed in order to investigate the regeneration mechanisms of bacteriorhodopsin (bR) from thermally unfolded bacterio-opsin (bO) and all-trans retinal. Regeneration kinetics data were successfully fitted to a single exponential function when regeneration was performed at 25 degrees C after incubation at high temperatures. Conversely, the process of regeneration after the addition of retinal to bO at high temperatures occurred at two different rate constants. These findings strongly suggest that the slower regeneration of bR at high temperatures occurs as a result of dynamic structural fluctuation of bO, whereas the faster process corresponds to regeneration from bO, which retains a native structure capable of retinal binding.

Bacteriorhodopsins↗
PubMed2005

Regeneration of bacteriorhodopsin from thermally unfolded bacterio-opsin and all-trans retinal at high temperatures.

The temperature dependence of regeneration of bacteriorhodopsin (bR) from its apoprotein, bacterio-opsin (bO), and all-trans retinal was investigated using two different procedures to probe the structural properties of bO at high temperatures. Regeneration experiments performed at 25 degrees C after incubation of bO within the temperature range of 35-75 degrees C indicate that irreversible thermal unfolding begins at 50 degrees C. When bO is incubated for one hour and mixed with retinal at the same elevated temperatures, however, a greater extent of regeneration to bR occurs, even at temperatures ranging from 50 to 65 degrees C. These experimental results indicate that regeneration of bR occurs from thermally unfolded bO and suggest dynamic structural fluctuation of bO in the unfolded state.

Bacteriorhodopsins↗
PubMed1994

[Pathology of opsins and vision disorders].

Mutations of the gene encoding rhodopsin are responsible for 30% of the cases autosomal dominant retinitis pigmentosa. Rhodopsin molecules are key G-coupled transmembrane proteins initiating the visual transduction cascade in rods. These cells are specialized retinal cells allowing the detection of low intensity lights. Mutations in the rhodopsin gene lead to the progressive destruction of rods, clinically translated by night blindness, a progressive bilateral loss of the peripheral visual field, and predominant alterations of the rod component of the electroretinograms. Inherited colour vision deficiencies are mainly caused by alterations of the genes encoding coloured opsins. These proteins are G-coupled receptors specialized in visual transduction in the cones. These sensorial cells are localized in the center of the neural retina where they allow the detection of refined details and chromatic lights. Rearrangements of the genes encoding the green and the red color pigments are responsible for daltonism.

Color Vision Defects↗
PubMed1976

Photosensitive pigments formed with rat opsin.

Photosensitive pigments are formed in vitro from rat opsin with the rods in suspension or as digitonin solutions. Rhodopsin, isorhodopsin I, and isorhodopsin II were generated with 11-cis, 9-cis and 9, 13-dicis retinal, respectively. An isorhodopsin I analogue was formed on combination with 9-cis 13-desmethyl-14-methylretinal. The absorption spectra and photosensitivities of these pigments were found to be similar to the corresponding bovine pigments although the rates of formation are several fold slower.

Animals↗
PubMed1995

Gene conversion between red and defective green opsin gene in blue cone monochromacy.

Blue cone monochromacy is an X-linked condition in which the function of both the red pigment gene (RCP) and the green pigment gene (GCP) is impaired. Blue cone monochromacy can be due to a red/green gene array rearrangement existing of a single red/green hybrid gene and an inactivating C203R point mutation in GCP. We describe here a family with blue cone monochromacy due to the presence of the C203R mutation in both RCP and GCP. The flanking sequences of the C203R mutation in exon 4 of RCP were characteristic for GCP, indicating that this mutation was transferred from GCP into RCP by gene conversion.

Base Sequence↗
PubMed1993

Subcellular localization of alpha-tubulin and opsin mRNA in the goldfish retina using digoxigenin-labeled cRNA probes detected by alkaline phosphatase and HRP histochemistry.

This paper describes a method for non-radioactive in situ hybridization providing subcellular localization of mRNA in 3 microns cryosections. We used two alternative colorimetric reactions to detect digoxigenin-labeled cRNA probes: alkaline phosphatase and HRP (horseradish peroxidase). With some probes the signal with the alkaline phosphatase reaction was intense, and diffusion of the reaction product was noticeable. Using HRP-conjugated antibodies improved the resolution but decreased the sensitivity of the signal. Photoamplification of the HRP reaction product increased the contrast and improved the sensitivity of the technique.

Alkaline Phosphatase↗
PubMed2004

Constitutive opsin signaling: night blindness or retinal degeneration?

A subset of genetic mutations in photoreceptor-specific genes results in abnormally prolonged activation of transducin-mediated photosignaling in rod cells. In humans and animal models, these mutations cause visual dysfunctions ranging from a mild stationary night blindness to severe, early-onset retinal degeneration. There are mechanistic differences between mutations causing night blindness and those causing retinal degeneration. Here, we hypothesize that mutations causing continuous activation of the visual cascade as the result, for example, of the inability of the photoreceptor to regenerate rhodopsin, lead to retinal degeneration; those mutations that can terminate signaling, even if only partially and intermittently, slow the rate of degeneration sufficiently to give rise to stationary night blindness. Furthermore, we hypothesize that a prolonged decrease in intracellular calcium concentration resulting from persistent activation is responsible for triggering apoptotic rod-cell death.

Animals↗