93 research outputs found
Tissue-type-specific heat-shock response and immunolocalization of class I low-molecular-weight heat-shock proteins in soybean.
No full textCloning and characterization of a cDNA-encoding an 18.0-kda class-1 low-molecular-weight heat-shock protein from rice.
No full textGO enrichment analyses of the hemichordate PFL chromosomes 9, 18, and 23 [Dataset]
No full textGO enrichment analyses of genes located on the specific chromosomes of the hemichordate PFL. The enriched GO terms (adjusted p-value <0.05) are clustered and divided into different modules. Descriptions of the most enriched GO terms of biological process (BP) within each module for genes located on PFL 9 (a), PFL18 (c), and PFL23 (e). The full list of enriched GO terms is provided in S4 Data. Results of the GO enrichment network analysis of genes located on PFL9 (b), PFL18 (d), and PFL23 (f). All labels are consistent with S17 Fig. The data underlying this figure can be found in S4 Data.Peer reviewe
Induction of a cDNA clone from rice encoding a class II small heat shock protein by heat stress, mechanical injury, and salicylic acid
No full textAcute Adaptation and Resetting of the Baroreflex Control of Vascular Resistance in the Canine Hindquarters and Mesentery
No full textThe Correlation of Cardiac Mass with Arterial Haemodynamics of Resistive and Capacitive Load in Arts with Normotension and Established Hypertension
No full textDistributions of TEs in amphioxus (BFL) and hemichordate (PFL) Hox-bearing chromosomes [Dataset]
No full textThe genome browser screenshots of the Hox-located chromosomes of BFL (a) and PFL (b). Histograms of all TEs (red), DNA transposons (DNA, yellow), long terminal repeats (LTR, green), long interspersed nuclear elements (LINE, blue), and short interspersed nuclear elements (SINE, purple) are shown. The bin size for each histogram of TEs is 50,000 bp or 10,000 bp (indicated on the left). Red boxes denote the genomic regions of the Hox clusters.Peer reviewe
Mechanistic insights into ethidium bromide removal by palygorskite from contaminated water
Full text linkEthidium bromide (EtBr)-containing wastewater can be hazardous to biodiversity when released into the soil and water bodies without treatment. EtBr can mutate living microbial cells and pose toxicity to even higher organisms. This work investigated the removal of EtBr from aqueous solutions by a naturally occurring palygorskite (PFl-1) clay mineral via systematic batch adsorption experiments under different physicochemical conditions. EtBr existed in an undissociated form at pH ~7, and was adsorbed on PFl-1 obeying the Freundlich isotherm model. The maximum EtBr adsorption capacity was 285 mmol/kg. The best fitted kinetic model for EtBr adsorption was the pseudo-second order model. The amounts of exchangeable cations desorbed from PFl-1 during EtBr adsorption was linearly correlated to the amounts of EtBr adsorbed, with a slope of 0.97, implying that a cation exchange-based adsorption mechanism was dominating. Additionally, dimerization of EtBr molecules via bromide release assisted an increased EtBr removal by PFl-1 at high adsorbate concentrations. Detailed x-ray diffraction, Fourier transform infrared, scanning electron imaging and energy dispersive x-ray analyses confirmed that EtBr adsorption occurred dominantly on the surface of palygorskite which mineralogically constituted 80% of the bulk PFl-1 adsorbent. A small portion of EtBr was also adsorbed by PFl-1 through intercalation onto the smectite impurity (10%) in PFl-1. This study suggested that PFl-1 could be an excellent natural material for removing EtBr from pharmaceutical and laboratory wastewater
Replacement of the Saccharomyces cerevisiae acetyl-CoA synthetases by alternative pathways for cytosolic acetyl-CoA synthesis
No full textCytosolic acetyl-coenzyme A is a precursor for many biotechnologically relevant compounds produced by Saccharomyces cerevisiae. In this yeast, cytosolic acetyl-CoA synthesis and growth strictly depend on expression of either the Acs1 or Acs2 isoenzyme of acetyl-CoA synthetase (ACS). Since hydrolysis of ATP to AMP and pyrophosphate in the ACS reaction constrains maximum yields of acetyl-CoA-derived products, this study explores replacement of ACS by two ATP-independent pathways for acetyl-CoA synthesis. After evaluating expression of different bacterial genes encoding acetylating acetaldehyde dehydrogenase (A-ALD) and pyruvate-formate lyase (PFL), acs1? acs2? S. cerevisiae strains were constructed in which A-ALD or PFL successfully replaced ACS. In A-ALD-dependent strains, aerobic growth rates of up to 0.27 h?1 were observed, while anaerobic growth rates of PFL-dependent S. cerevisiae (0.20 h?1) were stoichiometrically coupled to formate production. In glucose-limited chemostat cultures, intracellular metabolite analysis did not reveal major differences between A-ALD-dependent and reference strains. However, biomass yields on glucose of A-ALD- and PFL-dependent strains were lower than those of the reference strain. Transcriptome analysis suggested that reduced biomass yields were caused by acetaldehyde and formate in A-ALD- and PFL-dependent strains, respectively. Transcript profiles also indicated that a previously proposed role of Acs2 in histone acetylation is probably linked to cytosolic acetyl-CoA levels rather than to direct involvement of Acs2 in histone acetylation. While demonstrating that yeast ACS can be fully replaced, this study demonstrates that further modifications are needed to achieve optimal in vivo performance of the alternative reactions for supply of cytosolic acetyl-CoA as a product precursor.BT/BiotechnologyApplied Science
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