A5026928374- Photoreceptor and optogenetics research
- Photosynthetic Processes and Mechanisms
- Neuroscience and Neuropharmacology Research
- RNA and protein synthesis mechanisms
- Retinal Development and Disorders
- Genomics and Phylogenetic Studies
- bioluminescence and chemiluminescence research
- RNA Research and Splicing
- Cardiac Structural Anomalies and Repair
- Catalytic Cross-Coupling Reactions
- Circadian rhythm and melatonin
- Neuroscience and Neural Engineering
- Molecular Communication and Nanonetworks
- Nicotinic Acetylcholine Receptors Study
- Pharmacology and Obesity Treatment
- Asymmetric Hydrogenation and Catalysis
- Urinary Bladder and Prostate Research
- Additive Manufacturing and 3D Printing Technologies
- Algal biology and biofuel production
- Studies on Chitinases and Chitosanases
- Virus-based gene therapy research
- Chromosomal and Genetic Variations
- Microbial Metabolites in Food Biotechnology
- Sodium Intake and Health
- Viral Infections and Immunology Research
Nagoya Institute of Technology
2020-2024
Teikyo University Chiba Medical Center
2014-2021
Nagoya City University
2003
Nagoya University
1989-1999
Kyoto Prefectural University of Medicine
1985
National Institute of Genetics
1974
KCR channelrhodopsins (K
Rhodopsin phosphodiesterase (Rh-PDE) is an enzyme rhodopsin belonging to a recently discovered class of microbial rhodopsins with light-dependent enzymatic activity. Rh-PDE consists the N-terminal domain and C-terminal (PDE) domain, connected by 76-residue linker, hydrolyzes both cAMP cGMP in manner. Thus, has potential for optogenetic manipulation cyclic nucleotide concentrations, as complementary tool guanylyl cyclase photosensitive adenylyl cyclase. Here we present structural functional...
The 5'-terminal nucleotide sequences of human reovirus double-stranded RNA were determined after labeling the with [(32)P]phosphate by polynucleotide kinase. 5' terminal labeled to only a limited extent prior sequential oxidation, beta-elimination, and phosphomonoesterase treatment, indicating that phosphates in modified, blocked configuration. Each genome segment, removing blocking group, contained same two sequences: GpApUp one chain G(*)pCp other. G(*)p is derivative guanylic acid,...
Tobacco chloroplasts possess five conserved ribonucleoproteins (cpRNPs). To elucidate the function of cpRNPs we analyzed their localization and target nucleic acid molecules in chloroplasts. Immunoprecipitation stromal extract Northern analysis revealed that are associated vivo with not only various species chloroplast mRNAs but also intron‐containing precursor (pre‐) tRNAs. This observation strongly suggests involved RNA processing, including mRNA stability pre‐tRNA splicing.
Microbial and animal rhodopsins possess retinal chromophores which capture light normally photoisomerize from all-trans to 13-cis 11-cis all-trans-retinal, respectively. Here, we show that a near-infrared light-absorbing enzymerhodopsin Obelidium mucronatum (OmNeoR) contains the form in dark but isomerizes into 7-cis upon illumination. The photoproduct (λmax = 372 nm; P372) possesses deprotonated Schiff base, system exhibits bistable nature. photochemistry of OmNeoR was arrested at <270 K,...
Function of animal and microbial rhodopsins starts by light absorption the retinal chromophore. The maximum wavelength (λmax) is determined energy gap between electronically ground (S0) first excited (S1) state chromophore, color tuning mechanism one central topics in rhodopsin research. "Color switches", color-determining residues, are red- blue-shifting amino acids at same position two rhodopsins, whose exchange causes spectral blue- red-shifts, respectively, each rhodopsin. As mutation...
Rhodopsins are photoreceptive membrane proteins containing 11-cis (animal rhodopsins) and all-trans (microbial retinal chromophores. Animal rhodopsins act as G protein–coupled receptors, whereas microbial serve numerous roles can light-driven ion pumps, photosensors, light-gated channels, light-activated enzymes. Microbial play crucial in optogenetics. Isomerization is a shape-changing reaction that does not occur at low temperatures. In contrast, primary photo-intermediates formed even 77...
Five ribonucleoproteins (or RNA-binding proteins) from tobacco chloroplasts have been identified to date; each of these contains an acidic N-terminal domain (24–64 amino acids) and two conserved domains (82–83 acids). All five can bind ssDNA dsDNA but show high specificity for poly(G) poly(U). Here we present the nucleic acid binding activity using a series deletion mutant proteins made in vitro chloroplast 29 kDa ribonucleoproteins. The does not positive effect on activities lacking this...
We have previously identified three chloroplast ribonucleoproteins and characterized their cDNAs. Here we present the genomic organization, sequence expression of one genes. The 31 kd ribonucleoprotein (cp31) from tobacco (Nicotiana sylvestris) chloroplasts is coded for by a single-copy nuclear gene. This gene was isolated its determined. contains four exons introns. position first intron conserved among genes maize abscisic acid-induced glycine-rich protein, human hnRNP A1 protein cp31....
The choanoflagellate Salpingoeca rosetta contains a chimeric rhodopsin protein composed of an N-terminal (Rh) domain and C-terminal cyclic nucleotide phosphodiesterase (PDE) domain. Rh-PDE enzyme (SrRh-PDE), which decreases the concentrations nucleotides such as cGMP cAMP in light, is useful tool optogenetics. Recently, eight additional enzymes were found species, four from Choanoeca flexa other species. In this paper, we studied molecular properties these new Rh-PDEs, compared with...
For the quantitative measurement of pancreatic oncofetal antigen (POA), an enzyme immunoassay for POA has been developed, and is based on sandwich method using antibody-coupled glass beads (peroxidase)-labelled antibody. Serum concentrations were increased significantly in patients with cancer, but not those chronic pancreatitis or other miscellaneous diseases, normal subjects. It concluded that could be used assay our results show determination serum would useful diagnosis cancer.
Abstract Rhodopsin phosphodiesterase (Rh-PDE) is an enzyme rhodopsin belonging to a recently discovered class of microbial rhodopsins with light-dependent enzymatic activity. Rh-PDE consists the N-terminal domain and C-terminal (PDE) domain, connected by 76-residue linker, hydrolyzes both cAMP cGMP in manner. Thus, has potential for optogenetic manipulation cyclic nucleotide concentrations, as complementary tool guanylyl cyclase (Rh-GC) photosensitive adenylyl (PAC). Here we present...
Heliorhodopsin (HeR) is a new rhodopsin family discovered in 2018 through functional metagenomic analysis. Similar to microbial rhodopsins, HeR has an all-trans retinal chromophore, and its photoisomerization the 13-cis form triggers relatively slow photocycle with sequential intermediate states (K, M, O intermediates). The long lifetime putative active state for transferring signals or regulating enzymatic reactions. Although first HeR, 48C12, was found bacteria second (TaHeR) archaea,...
Abstract Photoisomerization is a key photochemical reaction in microbial and animal rhodopsins. It well established that such photoisomerization highly selective; all- trans to 13- cis , 11- forms rhodopsins, respectively. Nevertheless, unusual pathways have been discovered recently In an enzymerhodopsin NeoR, the chromophore isomerized into 7- form exclusively, which stable at room temperature. Although, produced by illumination of retinal, formation was never reported for protonated Schiff...
Tobacco chloroplast ribosomal protein L12 was isolated as a ssDNA‐cellulose‐binding from soluble fraction. Based on the N‐terminal amino acid sequence of L12, cDNA clone and characterized. The precursor deduced DNA consists transit peptide 53 residues mature 133 residues. synthesized with reticulocyte lysate subjected to nucleic acid‐binding assays. in vitro does not bind ssDNA, dsDNA nor ribonucleotide homopolymers, but it binds cellulose matrix.