Phonological memory in sign language relies on the visuomotor neural system outside the left hemisphere language network

Sign language is an essential medium for everyday social interaction for deaf people and plays a critical role in verbal learning. In particular, language development in those people should heavily rely on the verbal short-term memory (STM) via sign language. Most previous studies compared neural activations during signed language processing in deaf signers and those during spoken language processing in hearing speakers. For sign language users, it thus remains unclear how visuospatial inputs are converted into the verbal STM operating in the left-hemisphere language network. Using functional magnetic resonance imaging, the present study investigated neural activation while bilinguals of spoken and signed language were engaged in a sequence memory span task. On each trial, participants viewed a nonsense syllable sequence presented either as written letters or as fingerspelling (4–7 syllables in length) and then held the syllable sequence for 12 s. Behavioral analysis revealed that participants relied on phonological memory while holding verbal information regardless of the type of input modality. At the neural level, this maintenance stage broadly activated the left-hemisphere language network, including the inferior frontal gyrus, supplementary motor area, superior temporal gyrus and inferior parietal lobule, for both letter and fingerspelling conditions. Interestingly, while most participants reported that they relied on phonological memory during maintenance, direct comparisons between letters and fingers revealed strikingly different patterns of neural activation during the same period. Namely, the effortful maintenance of fingerspelling inputs relative to letter inputs activated the left superior parietal lobule and dorsal premotor area, i.e., brain regions known to play a role in visuomotor analysis of hand/arm movements. These findings suggest that the dorsal visuomotor neural system subserves verbal learning via sign language by relaying gestural inputs to the classical left-hemisphere language network

Large-scale mapping observations of the CI(3P1-3P0) and CO(J=3-2) lines toward the Orion A molecular cloud

Large scale mapping observations of the 3P1-3P0 fine structure transition of atomic carbon (CI, 492 GHz) and the J=3-2 transition of CO (346 GHz) toward the Orion A molecular cloud have been carried out with the Mt. Fuji submillimeter-wave telescope. The observations cover 9 square degrees, and include the Orion nebula M42 and the L1641 dark cloud complex. The CI emission extends over almost the entire region of the Orion A cloud and is surprisingly similar to that of 13CO(J=1-0).The CO(J=3-2) emission shows a more featureless and extended distribution than CI.The CI/CO(J=3-2) integrated intensity ratio shows a spatial gradient running from the north (0.10) to the south (1.2) of the Orion A cloud, which we interpret as a consequence of the temperature gradient. On the other hand, the CI/13CO(J=1-0) intensity ratio shows no systematic gradient. We have found a good correlation between the CI and 13CO(J=1-0) intensities over the Orion A cloud. This result is discussed on the basis of photodissociation region models.Comment: Text file is 13 pages long, and 3 figure files (pdf format). NRO Report No. 508 (1999). University of Tokyo, Resceu 41/9

Immunobiotic feed developed with Lactobacillus delbrueckii subsp. delbrueckii TUA4408L and the soymilk by-product okara improves health and growth performance in pigs

Lactobacillus delbrueckii subsp. delbrueckii TUA4408L is able to differentially modulate the innate immune response of porcine intestinal epithelial cells triggered by TLR4 activation. This strain also has a remarkable ability to grow on plant substrates. These two immunological and biotechnological characteristics prompted us to evaluate whether the soymilk by-product okara fermented with the TUA4408L strain can serve as an immunobiotic feed with the ability to beneficially modulate the intestinal immunity of piglets after weaning to improve their productivity. Our in vivo studies demonstrated that the administration of immunobiotic TUA4408L-fermented okara feed significantly increased piglet growth performance and meat quality. These positive effects were associated with the ability of the TUA4408L-fermented okara feed to beneficially modulate both intestinal microbiota and immunity in pigs. The immunobiotic feed improved the abundance of the beneficial bacteria Lactobacillus and Lactococcus in the gut of pigs, reduced blood markers of inflammation, and differentially regulated the expression of inflammatory and regulatory cytokines in the intestinal mucosa. These findings indicate that the immunobiotic TUA4408L-fermented okara feed could be an economical and environmentally friendly option to improve the growth performance and immune health of pigs.Fil: Suda, Yoshihito. Miyagi University; JapónFil: Sasaki, Nana. Miyagi University; JapónFil: Kagawa, Kyoma. Miyagi University; JapónFil: Elean, Mariano Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Zhou, Binghui. Tohoku University; JapónFil: Tomokiyo, Mikado. Tohoku University; JapónFil: Islam, Md Aminul. Tohoku University; Japón. Bangladesh Agricultural University; BangladeshFil: Shahid Riaz Rajoka, Muhammad. Tohoku University; JapónFil: Humayun Kober, A.K.M.. Tohoku University; Japón. Chittagong Veterinary and Animal Sciences University; BangladeshFil: Shimazu, Tomoyuki. Miyagi University; JapónFil: Egusa, Shintaro. No especifíca;Fil: Terashima, Yuji. No especifíca;Fil: Aso, Hisashi. Tohoku University; JapónFil: Ikeda Ohtsubo, Wakako. Tohoku University; JapónFil: Villena, Julio Cesar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Kitazawa, Haruki. Tohoku University; Japó

Isolation culture of the cold-adapted microorganis for polysaccharide producing

第2回極域科学シンポジウム/第33回極域生物シンポジウム 11月18日（金） 統計数理研究所 3階リフレッシュフロ

Synthesis and Characterization of Alkali Metal Ion-Binding Copolymers Bearing Dibenzo-24-crown-8 Ether Moieties

Dibenzo-24-crown-8 (DB24C8)-bearing copolymers were synthesized by radical copolymerization using a DB24C8-carrying acrylamide derivative and N-isopropylacrylamide monomers. The cloud point of the resulting copolymers changed in aqueous solution in the presence of cesium ions. In addition, the 1H NMR signals of DB24C8-bearing copolymers shifted in the presence of alkali metal. This shift was more pronounced following the addition of Cs+ compared to Rb+, K+, Na+, and Li+ ions due to recognition of the Cs+ ion by DB24C8

Immobilization of the iron on the surface of non-woven carbon fiber for use in a microbial fuel cell

Abstract Iron particles were immobilized onto non-woven carbon fiber via electroplating for use in a microbial fuel cell (MFC). Electroplating was performed under an applied voltage at a current of 0.2 A for 5, 10, and 15 min. The scanning electron microscope (SEM) observations show that 5 min was not adequate for the particles to be immobilized, whereas 10 and 15 min of electroplating resulted in an adequate number of particles on the surface. To evaluate the strength of the binding of iron via electroplating on the surface of the fiber, the samples were washed with pure water and observed using an SEM. The 10 min electroplated sample has a larger surface area, which is suitable for the MFC anode, than the 15 min electroplated sample. According to X-ray photoelectron spectroscopy and X-ray diffraction analysis, the peaks corresponded to those of Fe2O3, and the sample dipped into tannic acid shows the peaks of Fe3O4. The amount of biofilm of Shewanella oneidensis MR-1 was evaluated using crystal violet staining, and living bacteria were counted as colony forming units. Electroplated Fe2O3 and Fe3O4 were found to be effective for producing biofilm and immobilizing S. oneidensis MR-1

Cooperative Transport between NukFEG and NukH in Immunity against the Lantibiotic Nukacin ISK-1 Produced by Staphylococcus warneri ISK-1▿

Nukacin ISK-1 is a lantibiotic produced by Staphylococcus warneri ISK-1. Previous studies have reported that the self-protection system of the nukacin ISK-1 producer involves the cooperative function of the ABC transporter NukFEG and the lantibiotic-binding immunity protein NukH. In this study, the cooperative mechanism between NukFEG and NukH was characterized by using fluorescein-4-isothiocyanate (FITC)-labeled nukacin ISK-1 (FITC-nuk) to clarify the localization of nukacin ISK-1 in the immunity process. Lactococcus lactis recombinants expressing nukFEGH, nukFEG, or nukH showed immunity against FITC-nuk, suggesting that FITC-nuk was recognized by the self-protection system against nukacin ISK-1. Analysis of the interaction between FITC-nuk and energy-deprived cells of the L. lactis recombinants showed that FITC-nuk specifically bound to cells expressing nukH. The interaction between FITC-nuk and nukH-expressing cells was inhibited by the addition of unlabeled nukacin ISK-1 and its derivatives with deletions of the N-terminal tail region, but not by the addition of a synthesized N-terminal tail region. This suggests that the NukH protein recognizes the C-terminal ring region of nukacin ISK-1. The addition of glucose to nukFEGH-expressing cells treated with FITC-nuk resulted in a time-dependent decrease in fluorescence intensity, indicating that FITC-nuk was transported from the cell membrane by the NukFEG protein. These results revealed that after being captured by NukH in an energy-independent manner, nukacin ISK-1 was transported to the extracellular space by NukFEG in an energy-dependent manner

Lysine-Oriented Charges Trigger the Membrane Binding and Activity of Nukacin ISK-1

The antibacterial activities and membrane binding of nukacin ISK-1 and its fragments and mutants were evaluated to delineate the determinants governing structure-function relationships. The tail region (nukacin(1-7)) and ring region (nukacin(7-27)) were shown to have no antibacterial activity and also had no synergistic effect on each other or even on nukacin ISK-1. Both a fragment with three lysines in the N terminus deleted (nukacin(4-27)) and a mutant with three lysines in the N terminus replaced with alanine (K1-3A nukacin ISK-1) imparted very low activity (32-fold lower than nukacin ISK-1) and also exhibited a similar antagonistic effect on nukacin ISK-1. Addition of two lysine residues at the N terminus (+2K nukacin ISK-1) provided no further increased antibacterial activity. Surface plasmon resonance sensorgrams and kinetic rate constants determined by a BIAcore biosensor revealed that nukacin ISK-1 has remarkably higher binding affinity to anionic model membrane than to zwitterionic model membrane. Similar trends of strong binding responses and kinetics were indicated by the high affinities of nukacin ISK-1 and +2K nukacin ISK-1, but there was no binding of tail region, ring region, nukacin(4-27), and K1-3A nukacin ISK-1 to the anionic model membrane. Our findings therefore suggest that the complete structure of nukacin ISK-1 is necessary for its full activity, in which the N-terminus three lysine residues play a crucial role in electrostatic binding to the target membrane and therefore nukacin ISK-1's ability to exert its potent antibacterial activity

Production of Glyoxylate from Glucose in Engineered <i>Escherichia coli</i>

Glyoxylates are essential intermediates in several metabolic pathways and have a broad range of industrial applications. In this study, we propose a novel method for producing glyoxylate from glucose using engineered Escherichia coli BW25113. To direct the production of glyoxylate from glucose, malate synthase A (aceB), malate synthase G (glcB), glyoxylate carboligase (gcl), and glyoxylate/hydroxypyruvate reductase A (ycdW) genes were disrupted, and the glyoxylate shunt was reinforced in the disruptants by the overexpression of citrate synthase (gltA) and isocitrate lyase (aceA). In flask cultivation using M9 medium supplemented with 1% glucose, the disruptant E. coli BW25113 ΔaceB ΔglcB Δgcl ΔycdW produced 0.93 ± 0.17 g/L of glyoxylate. Further overexpression of gltA and aceA in the disruptant resulted in an improvement in glyoxylate production to 1.15 ± 0.02 g/L. By expressing a heterologous gene, pyc, in the engineered E. coli, the accumulation of intracellular oxaloacetate remarkably improved, leading to glyoxylate production of up to 2.42 ± 0.00 g/L with specific productivity at 4.22 ± 0.09 g/g-cell. To date, this is the highest reported titer and specific productivity of glyoxylate in E. coli