Tokyo University of Science

About: Tokyo University of Science is a education organization based out in Tokyo, Japan. It is known for research contribution in the topics: Catalysis & Thin film. The organization has 15800 authors who have published 24147 publications receiving 438081 citations. The organization is also known as: Tōkyō Rika Daigaku & Science University of Tokyo.

DELLAs Function as Coactivators of GAI-ASSOCIATED FACTOR1 in Regulation of Gibberellin Homeostasis and Signaling in Arabidopsis

Abstract: Gibberellins (GAs) are essential regulators of plant development, and DELLAs are negative regulators of GA signaling. The mechanism of GA-dependent transcription has been explained by DELLA-mediated titration of transcriptional activators and their release through the degradation of DELLAs in response to GA. However, the effect of GA on genome-wide expression is predominantly repression, suggesting the existence of unknown mechanisms of GA function. In this study, we identified an Arabidopsis thaliana DELLA binding transcription factor, GAI-ASSOCIATED FACTOR1 (GAF1). GAF1 shows high homology to INDETERMINATE DOMAIN1 (IDD1)/ENHYDROUS. GA responsiveness was decreased in the double mutant gaf1 idd1, whereas it was enhanced in a GAF1 overexpressor. GAF1 binds to genes that are subject to GA feedback regulation. Furthermore, we found that GAF1 interacts with the corepressor TOPLESS RELATED (TPR) and that DELLAs and TPR act as coactivators and a corepressor of GAF1, respectively. GA converts the GAF1 complex from transcriptional activator to repressor via the degradation of DELLAs. These results indicate that DELLAs turn on or off two sets of GA-regulated genes via dual functions, namely titration and coactivation, providing a mechanism for the integrative regulation of plant growth and GA homeostasis.

Deaminase-mediated multiplex genome editing in Escherichia coli

Abstract: In eukaryotes, the CRISPR-Cas9 system has now been widely used as a revolutionary genome engineering tool1, 2. However, in prokaryotes, the use of nuclease-mediated genome editing tools has been limited to negative selection for the already modified cells because of its lethality3, 4. Here, we report on deaminase-mediated targeted nucleotide editing (Target-AID) 5 adopted in Escherichia coli. Cytidine deaminase PmCDA1 fused to the nuclease-deficient CRISPR-Cas9 system achieved specific point mutagenesis at the target sites in E. coli by introducing cytosine mutations without compromising cell growth. The cytosine-to-thymine substitutions were induced mainly within an approximately five-base window of target sequences on the protospacer adjacent motif-distal side, which can be shifted depending on the length of the single guide RNA sequence. Use of a uracil DNA glycosylase inhibitor 6 in combination with a degradation tag (LVA tag) 7 resulted in a robustly high mutation efficiency, which allowed simultaneous multiplex editing of six different genes. The major multi-copy transposase genes that consist of at least 41 loci were also simultaneously edited by using four target sequences. As this system does not rely on any additional or host-dependent factors, it may be readily applicable to a wide range of bacteria.

Superconductivity and Structural Phase Transitions in Caged Compounds RT2Zn20 (R = La, Pr, T = Ru, Ir)

Abstract: Electrical resistivity ρ, specific heat C , magnetization M measurements are reported on four compounds, LaRu 2 Zn 20 , PrRu 2 Zn 20 , LaIr 2 Zn 20 , and PrIr 2 Zn 20 , which crystallize in a cubic CeCr 2 Al 20 -type structure. LaRu 2 Zn 20 , LaIr 2 Zn 20 , and PrIr 2 Zn 20 show superconducting transitions at T C = 0.2, 0.6, and ∼0.05 K, respectively, whereas PrRu 2 Zn 20 remains a normal state down to 0.04 K. This is the first observation of superconductivity in the family of RT 2 X 20 (T = transition metal; X = Al and Zn). Furthermore, structural phase transitions manifest themselves at T s = 150, 138, and 200 K for LaRu 2 Zn 20 , PrRu 2 Zn 20 , and LaIr 2 Zn 20 , respectively. No magnetic transition is found in PrRu 2 Zn 20 and PrIr 2 Zn 20 down to 1.8 K. On cooling PrIr 2 Zn 20 below 2 K, the specific heat divided by temperature, C / T , continuously increases and reaches 5 J/(K 2 ·mol) at 0.4 K, suggesting that Pr 4 f 2 electrons are involved in the heavy-fermion state, as observed in a related compo...

The Cobalt Porphyrin−Lewis Base System: A Highly Selective Catalyst for Alternating Copolymerization of CO2 and Epoxide under Mild Conditions

Abstract: The use of a cobalt porphyrin ((TPP)CoCl, 1) in combination with dimethylaminopyridine (DMAP) for the alternating copolymerization of CO2 and epoxide is described. The (TPP)CoCl (1)−DMAP system quantitatively produced the alternating copolymer from CO2 and cyclohexene oxide (CHO) under optimized conditions (50 atm, 80 °C). This calatyst system also worked satisfactorily for the alternating copolymerization of CO2 and a terminal epoxide, e.g., propylene oxide (PO), without formation of cyclic carbonate to give the polycarbonate. The alternating copolymerization of CO2 and epoxide (CHO, PO) was achieved under very mild conditions, such as at ambient temperature and under CO2 at 1 atm, by using the 1−DMAP catalyst system.

The novel β-secretase inhibitor KMI-429 reduces amyloid β peptide production in amyloid precursor protein transgenic and wild-type mice

Abstract: Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid plaques and neurofibrillary tangles in the brain. The major component of the plaques, amyloid beta peptide (Abeta), is generated from amyloid precursor protein (APP) by beta- and gamma-secretase-mediated cleavage. Because beta-secretase/beta-site APP cleaving enzyme 1 (BACE1) knockout mice produce much less Abeta and grow normally, a beta-secretase inhibitor is thought to be one of the most attractive targets for the development of therapeutic interventions for AD without apparent side-effects. Here, we report the in vivo inhibitory effects of a novel beta-secretase inhibitor, KMI-429, a transition-state mimic, which effectively inhibits beta-secretase activity in cultured cells in a dose-dependent manner. We injected KMI-429 into the hippocampus of APP transgenic mice. KMI-429 significantly reduced Abeta production in vivo in the soluble fraction compared with vehicle, but the level of Abeta in the insoluble fraction was unaffected. In contrast, an intrahippocampal injection of KMI-429 in wild-type mice remarkably reduced Abeta production in both the soluble and insoluble fractions. Our results indicate that the beta-secretase inhibitor KMI-429 is a promising candidate for the treatment of AD.