A5091272822- Endoplasmic Reticulum Stress and Disease
- Bacterial Genetics and Biotechnology
- Redox biology and oxidative stress
- Laser Applications in Dentistry and Medicine
- RNA and protein synthesis mechanisms
- Bacteriophages and microbial interactions
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Pancreatic function and diabetes
- Periodontal Regeneration and Treatments
- Cellular transport and secretion
- Hops Chemistry and Applications
- Polyamine Metabolism and Applications
- Bone and Dental Protein Studies
- dental development and anomalies
- Enzyme Production and Characterization
- RNA regulation and disease
- Photosynthetic Processes and Mechanisms
- Viral gastroenteritis research and epidemiology
- Hemoglobin structure and function
- Adenosine and Purinergic Signaling
- Heat shock proteins research
- Computational Drug Discovery Methods
- Autophagy in Disease and Therapy
- Biochemical Analysis and Sensing Techniques
Tohoku University
2013-2024
Nara Institute of Science and Technology
2009-2024
Meikai University
2000-2024
Institute of Science Tokyo
2024
Rockefeller University
2019
Institute for Multidisciplinary Research
2017
Ohu University
2012
Harvard University
2001-2012
Osaka University
2011
University of Michigan
2000-2004
Upon endoplasmic reticulum (ER) stress, an endoribonuclease, inositol-requiring enzyme-1α, splices the precursor unspliced form of X-box-binding protein 1 messenger RNA (XBP1u mRNA) on ER membrane to yield active transcription factor (XBP1s), leading alleviation stress. The nascent peptide encoded by XBP1u mRNA drags mRNA-ribosome-nascent chain (R-RNC) complex for efficient cytoplasmic splicing. We found that translation was briefly paused stabilize R-RNC complex. Mutational analysis...
DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed complexes between DsbA and its substrates. However, these are difficult detect, probably because their short-lived nature. Here we show that it possible detect such covalent intermediates in vivo by mutation alters cis proline-151. Further, this mutant allowed us identify substrates DsbA. Alteration the proline, highly conserved among...
In mammals, the prototypical endoplasmic reticulum (ER) stress sensor inositol-requiring enzyme 1 (IRE1) has diverged into two paralogs. IRE1 α is broadly expressed and mediates unconventional splicing of X-box binding protein (XBP1) mRNA during ER stress. By contrast, IRE1β selectively in digestive tract, its function remains unclear. Here, we report that plays a distinctive role mucin-secreting goblet cells. −/− mice, aberrant mucin 2 (MUC2) accumulated cells, accompanied by distension...
In mammalian pancreatic β cells, the IRE1α–XBP1 pathway is constitutively and highly activated under physiological conditions. To elucidate precise role of this pathway, we constructed cell–specific Ire1α conditional knockout (CKO) mice established insulinoma cell lines in which was deleted using Cre–loxP system. CKO showed typical diabetic phenotype including impaired glycemic control defects insulin biosynthesis postnatally at 4–20 weeks. deletion cells resulted decreased secretion,...
We determined the nucleotide sequence of a 1.9-kilobase fragment Pseudomonas paucimobilis SYK6 chromosomal DNA that included genes encoding protocatechuate 4,5-dioxygenase, enzyme responsible for aromatic ring fission protocatechuate. Two open reading frames 417 and 906 base pairs were found had no homology with previously reported sequences, including those 3,4-dioxygenase. Since both indispensable activity, they should encode subunits 4,5-dioxygenase. named these ligA ligB. Protocatechuate...
Get Ready, Assemble, Fold The outer membrane protein complex LptD/E is responsible for lipopolysaccharide export to the cell surface of Escherichia coli. LptD an essential β-barrel that contains two disulfide bonds between nonconsecutive cysteines. Chng et al. (p. 1665 , published online 30 August) describe characterization oxidative folding and assembly pathway in living cells. A combination steady-state pulse-chase measurements was used identify seven intermediates with different...
Cytosolic Hsc70/Hsp70 are known to contribute the endoplasmic reticulum (ER)-associated degradation of membrane proteins. However, at least in mammalian cells, its partner ER-localized J-protein for this cellular event has not been identified. Here we propose that missing protein is DNAJB12. Protease protection assay and immunofluorescence study revealed DNAJB12 an single membrane-spanning carrying a J-domain facing cytosol. Using co-immunoprecipitation assay, found able bind Hsc70 thus can...
Oxidative protein folding occurs primarily in the mammalian endoplasmic reticulum, enabled by a diverse network comprising more than 20 members of disulfide isomerase (PDI) family and five PDI oxidases. Although canonical bond formation pathway involving Ero1α has been well-studied so far, physiological roles newly identified oxidases, glutathione peroxidase-7 (GPx7) -8 (GPx8), are only poorly understood. We here demonstrated that human GPx7 much higher reactivity with H2O2 hence greater...
AbstractA new method for determining the capability of beer-spoilage by lactobacilli was developed. This is based on sequence a hop possible-resistance gene, designated horA (1,749base), which identified plasmid hop-resistant Lactobacillus brevis ABBC45. A pair primers were designed partial horA. We examined various species presence horA-like gene polymerase chain reaction (PCR) using these primers. The amplification specific DNA fragments, suggests occurred almost exclusively in regardless...
We have isolated a Schizosaccharomyces pombe gene, bfr1+, which on multicopy plasmid vector, pDB248', confers resistance to brefeldin A (BFA), an inhibitor of intracellular protein transport. This gene encodes novel 1,531 amino acids with intramolecular duplicated structure, each half containing single ATP-binding consensus sequence and set six transmembrane sequences. structural characteristic bfr1+ resembles that mammalian P-glycoprotein, which, by exporting variety anticancer drugs, has...
The active-site cysteines of DsbA, the periplasmic disulfide-bond-forming enzyme Escherichia coli , are kept oxidized by cytoplasmic membrane protein DsbB. DsbB, in turn, is two kinds quinones (ubiquinone for aerobic and menaquinone anaerobic growth) electron-transport chain. We describe isolation dsbB missense mutations that change a highly conserved arginine residue at position 48 to histidine or cysteine. In these mutants, DsbB functions reasonably well aerobically but poorly...
Organisms have evolved elaborate systems that ensure the homeostasis of thiol redox environment in their intracellular compartments. In Escherichia coli, cytoplasm is kept under reducing conditions by thioredoxins with help thioredoxin reductase and glutaredoxins small molecule glutathione reductase. As a result, disulfide bonds are constantly resolved this compartment. contrast to cytoplasm, periplasm E. coli maintained an oxidized state DsbA, which recycled DsbB. Thioredoxin 1, when...
Several reports have shown that the photo-bio-modulation of cells by various lasers has favorable biological effects. However, effects low-level Er:YAG laser irradiation on osteoblasts remain unclear. The purpose this study was to evaluate proliferation and osteogenic differentiation primary osteoblast-like isolated from calvariae 3-5-day-old Wistar rats. Cells were irradiated at energy fluences 2.2, 3.3, 4.3 J/cm2, respectively. After irradiation, cell surface temperatures measured...