Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Halobacterium halobium contains at least three retinal-containing pigments: bacteriorhodopsin, halorhodopsin, and a third rhodopsin-like pigment (tR) absorbing at approximately 590 nm, tR590. Illumination of tR590 gives rise to a very long-lived blue absorbing photoproduct, tR370. Using high-performance liquid chromatography we show that the chromophore of tR590 is primarily all-trans retinal and its conversion by light to tR370 causes the chromophore to isomerize primarily to the 13-cis conformation. Irradiation of the tR370 gives rise to a transient photoproduct absorbing at approximately 520 nm that decays back to the initial pigment tR590. In addition to all-trans retinal, the apomembrane of tR can also combine with 13-cis retinal but not with the 9- or 11-cis isomers.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1435195PMC
http://dx.doi.org/10.1016/S0006-3495(85)83969-2DOI Listing

Publication Analysis

Top Keywords

third rhodopsin-like
8
rhodopsin-like pigment
8
halobacterium halobium
8
all-trans retinal
8
characterization chromophore
4
chromophore third
4
pigment halobacterium
4
halobium photoproduct
4
photoproduct halobacterium
4
halobium three
4

Similar Publications

Understanding the evolutionary relationship between immune cells and the blood-brain barrier (BBB) is important to devise therapeutic strategies. In vertebrates, immune cells follow either a paracellular or a transcellular pathway to infiltrate the BBB. In , glial cells form the BBB that regulates the access of hemocytes to the brain.

View Article and Find Full Text PDF

Preferential Coupling of Dopamine D and D Receptor Isoforms with G and G Proteins-In Silico Study.

Int J Mol Sci

January 2020

Department of Synthesis and Chemical Technology of Pharmaceutical Substances with Computer Modeling Laboratory, Faculty of Pharmacy, Medical University of Lublin, 4A Chodzki St., PL-20093 Lublin, Poland.

The dopamine D receptor belongs to rhodopsin-like G protein-coupled receptors (GPCRs) and it is an important molecular target for the treatment of many disorders, including schizophrenia and Parkinson's disease. Here, computational methods were used to construct the full models of the dopamine D receptor short (D) and long (D) isoforms (differing with 29 amino acids insertion in the third intracellular loop, ICL3) and to study their coupling with G and G proteins. It was found that the D isoform preferentially couples with the G protein and D isoform with the G protein, which is in accordance with experimental data.

View Article and Find Full Text PDF

Mutations in GPR101 as a potential cause of X-linked acrogigantism and acromegaly.

Prog Mol Biol Transl Sci

August 2019

Department of Anatomy, Physiology and Pharmacology, College of Veterinary Medicine, Auburn University, Auburn, AL, United States; Center for Neuroscience Initiative, Auburn University, Auburn, AL, United States. Electronic address:

X-linked acrogigantism (XLAG) is a recently described early-onset gigantism due to GPR101 duplication that induces growth hormone (GH) oversecretion. GPR101, which belongs to Family A rhodopsin-like family of G protein-coupled receptors, is predominantly expressed in hypothalamus and pituitary, suggesting that GPR101 might be important in regulating diverse functions such as energy balance and reproduction. Most mammalian GPR101s have extremely long third intracellular loops (ICL3); however, zebrafish GPR101 has a much shorter ICL3, but a longer C-terminus.

View Article and Find Full Text PDF

In this study, a long neuropeptide F receptor of the blood-feeding hemipteran, Rhodnius prolixus (RhoprNPFR) has been cloned and characterized. Approximately 70% of the RhoprNPFR deduced protein sequence is identical to that of other hemipteran NPFRs. RhoprNPFR has seven highly-conserved transmembrane domains, two cysteine residues in the 2nd and 3rd extracellular loops that likely form a disulfide bond integral for maintaining the structure of the receptor, and a conserved DRY motif after the third transmembrane domain.

View Article and Find Full Text PDF

The comprehensive expression analysis of the G protein-coupled receptor from Penaeus monodon indicating it participates in innate immunity and anti-ammonia nitrogen stress.

Fish Shellfish Immunol

April 2018

South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Key Laboratory of South China Sea Fishery Resources Exploitation and Utilization, Ministry of Agriculture, Guangzhou, 510300, PR China; Shenzhen Base of South China Sea Fisheries Research Institute, Chinese Academy of

The G protein-coupled receptors (GPCRs) composed a superfamily that played an important role in physiological processes of crustaceans, with multiple functions such as growth and development, acting as a defense against stimulations from external factors. In this paper, one kind of GPCRs were identified from Penaeus monodon, called PmGPCR, included an open reading frame (ORF) of 1113 bp. Bioinformatic analysis showed that PmGPCR protein had the typical structure of seven transmembrane domains (7TM), especially the special Asp-Arg-Try motif (DRY motif) between the third transmembrane structures (TM3) and the second intracellular loops (IL-2) which can prove that PmGPCR belongs to the rhodopsin-like family.

View Article and Find Full Text PDF