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Nanoscale Advances Nov 2022In the energy storage field, an electrode material must possess both good ionic and electronic conductivities to perform well, especially when high power is needed. In...
In the energy storage field, an electrode material must possess both good ionic and electronic conductivities to perform well, especially when high power is needed. In this context, the development of composite electrode materials combining an electrochemically active and good ionic conductor phase with an electronic conductor appears as a perfectly adapted approach to generate a synergetic effect and optimize the energy storage performance. In this work, three layered MnO phases with various morphologies (veils, nanoplatelets and microplatelets) were combined with electronic conductor cobalt oxyhydroxides with different platelet sizes (∼20 nm 70 nm wide), to synthesize 6 different composites by exfoliation and restacking processes. The influence of precursors' morphology on the distribution of the Mn and Co objects within the composites was carefully investigated and correlated with the electrochemical performance of the final restacked material. Overall, the best performing restacked composite was obtained by combining MnO possessing a veil morphology with the smallest cobalt oxyhydroxide nanoplatelets, leading to the most homogeneous distribution of the Mn and Co objects at the nanoscale. More generally, the aim of this work is to understand how the size and morphology of the precursor building blocks influence their distribution homogeneity within the final composite and to find the most compatible building blocks to reach a homogeneous distribution at the nanoscale.
PubMed: 36504748
DOI: 10.1039/d2na00616b -
The Journal of Biological Chemistry Jul 1991Secretin is a 27-amino acid gastrointestinal hormone that stimulates the secretion of bicarbonate-rich pancreatic fluid. We isolated and analyzed the coding region of...
Secretin is a 27-amino acid gastrointestinal hormone that stimulates the secretion of bicarbonate-rich pancreatic fluid. We isolated and analyzed the coding region of the gene for the rat secretin precursor. The entire coding region spans 692 base pairs and is divided into four regions corresponding to the signal peptide and NH2-terminal peptide, the secretin peptide and processing signal sequences, a part of the COOH-terminal peptide, and the remainder of the COOH-terminal peptide, which are interrupted by three short introns (81, 105, and 104 base pairs). The organization is similar to those of the genes for other members of the secretin family, glucagon and VIP/PHI-27 precursors, supporting the assumption that the genes for the secretin family peptide precursors originated from a common ancestral gene. We also demonstrated that the secretin precursor gene is widely expressed in the brain and in the hypophysis. The regional expression pattern of the secretin precursor gene in the brain is quite different from those of the glucagon and VIP/PHI-27 precursor genes. The secretin precursor gene is highly expressed in the medulla oblongata and pons of the brain and the hypophysis, the expression levels of which are comparable to those in the duodenum. The secretin precursor mRNA in the brain and the hypophysis has the same coding sequence as that in the duodenum, indicating that secretin in the brain and the hypophysis is produced from the same secretin precursor protein as that in the duodenum. This is the first evidence to be reported that the secretin precursor gene is definitely expressed in the brain.
Topics: Amino Acid Sequence; Animals; Base Sequence; Brain Chemistry; Duodenum; Electrophoresis, Agar Gel; Molecular Sequence Data; Pituitary Gland, Anterior; Polymerase Chain Reaction; Protein Precursors; RNA, Messenger; Rats; Restriction Mapping; Secretin
PubMed: 2061329
DOI: No ID Found -
PLoS Computational Biology Apr 202013C-metabolic flux analysis (13C-MFA) allows metabolic fluxes to be quantified in living organisms and is a major tool in biotechnology and systems biology. Current...
13C-metabolic flux analysis (13C-MFA) allows metabolic fluxes to be quantified in living organisms and is a major tool in biotechnology and systems biology. Current 13C-MFA approaches model label propagation starting from the extracellular 13C-labeled nutrient(s), which limits their applicability to the analysis of pathways close to this metabolic entry point. Here, we propose a new approach to quantify fluxes through any metabolic subnetwork of interest by modeling label propagation directly from the metabolic precursor(s) of this subnetwork. The flux calculations are thus purely based on information from within the subnetwork of interest, and no additional knowledge about the surrounding network (such as atom transitions in upstream reactions or the labeling of the extracellular nutrient) is required. This approach, termed ScalaFlux for SCALAble metabolic FLUX analysis, can be scaled up from individual reactions to pathways to sets of pathways. ScalaFlux has several benefits compared with current 13C-MFA approaches: greater network coverage, lower data requirements, independence from cell physiology, robustness to gaps in data and network information, better computational efficiency, applicability to rich media, and enhanced flux identifiability. We validated ScalaFlux using a theoretical network and simulated data. We also used the approach to quantify fluxes through the prenyl pyrophosphate pathway of Saccharomyces cerevisiae mutants engineered to produce phytoene, using a dataset for which fluxes could not be calculated using existing approaches. A broad range of metabolic systems can be targeted with minimal cost and effort, making ScalaFlux a valuable tool for the analysis of metabolic fluxes.
Topics: Carbon Isotopes; Metabolic Engineering; Metabolic Flux Analysis; Metabolic Networks and Pathways; Models, Biological; Polyisoprenyl Phosphates; Saccharomyces cerevisiae; Systems Biology; Terpenes
PubMed: 32287281
DOI: 10.1371/journal.pcbi.1007799 -
Foods (Basel, Switzerland) Mar 2023The metabolic modulation of major flavor precursors during coffee cherry ripening is critical for the characteristic coffee flavor formation. However, the formation...
The metabolic modulation of major flavor precursors during coffee cherry ripening is critical for the characteristic coffee flavor formation. However, the formation mechanism of flavor precursors during coffee cherry ripening remains unknown. In the present study, a colorimeter was employed to distinguish different maturity stages of coffee cherry based on the coffee cherry skin colors, and proteomics and metabolomics profiles were integrated to comprehensively investigate the flavor precursor dynamics involved in Arabica coffee cherry ripening. The data obtained in the present study provide an integral view of the critical pathways involved in flavor precursor changes during coffee cherry ripening. Moreover, the contributions of critical events in regulating the development of flavor precursors during the four ripening stages of coffee cherries, including the biosynthesis and metabolism pathways of organic acids, amino acids, flavonoids, and sugars, are discussed. Overall, a total of 456 difference express metabolites were selected, and they were identified as being concentrated in the four maturity stages of coffee cherries; furthermore, 76 crucial enzymes from the biosynthesis and metabolism of sugars, organic acids, amino acids, and flavonoids contributed to flavor precursor formation. Among these enzymes, 45 difference express proteins that could regulate 40 primary amino acids and organic acids flavor precursors were confirmed. This confirmation indicates that the metabolic pathways of amino acids and organic acids played a significant role in the flavor formation of Arabica coffee cherries during ripening. These results provide new insights into the protease modulation of flavor precursor changes in Arabica coffee cherry ripening.
PubMed: 37048253
DOI: 10.3390/foods12071432 -
Plant Physiology Feb 2013Proteins destined for the thylakoid lumen of chloroplasts must cross three membranes en route. The chloroplast twin arginine translocation (cpTat) system facilitates the...
Proteins destined for the thylakoid lumen of chloroplasts must cross three membranes en route. The chloroplast twin arginine translocation (cpTat) system facilitates the transport of about one-half of all proteins that cross the thylakoid membrane in chloroplasts. Known mechanistic features of the cpTat system are drastically different from other known translocation systems, notably in its formation of a transient complex to transport fully folded proteins utilizing only the protonmotive force generated during photosynthesis for energy. However, key details, such as the structure and composition of the translocation pore, are still unknown. One of the three transmembrane cpTat components, Tha4, is thought to function as the pore by forming an oligomer. Yet, little is known about the topology of Tha4 in thylakoid, and little work has been done to detect precursor-Tha4 interactions, which are expected if Tha4 is the pore. Here, we present evidence of the interaction of the precursor with Tha4 under conditions leading to transport, using cysteine substitutions on the precursor and Tha4 and disulfide bond formation in pea (Pisum sativum). The mature domain of a transport-competent precursor interacts with the amphipathic helix and amino terminus of functional Tha4 under conditions leading to transport. Detergent solubilization of thylakoids post cross linking and blue-native polyacrylamide gel electrophoresis analysis shows that Tha4 is found in a complex containing precursor and Hcf106 (i.e. the cpTat translocase). Affinity precipitation of the cross-linked complex via Tha4 clearly demonstrates that the interaction is with full-length precursor. How these data suggest a role for Tha4 in cpTat transport is discussed.
Topics: Amino Acid Substitution; Binding Sites; Cysteine; Electrophoresis; Membrane Proteins; Models, Molecular; Mutation; Plant Proteins; Protein Binding; Protein Precursors; Protein Structure, Tertiary; Protein Transport; Thylakoids
PubMed: 23209125
DOI: 10.1104/pp.112.207522 -
Nucleic Acids Research Jun 2019In most bacteria, ribosomal RNA is transcribed as a single polycistronic precursor that is first processed by RNase III. This double-stranded specific RNase cleaves two...
In most bacteria, ribosomal RNA is transcribed as a single polycistronic precursor that is first processed by RNase III. This double-stranded specific RNase cleaves two large stems flanking the 23S and 16S rRNA mature sequences, liberating three 16S, 23S and 5S rRNA precursors, which are further processed by other ribonucleases. Here, we investigate the rRNA maturation pathway of the human gastric pathogen Helicobacter pylori. This bacterium has an unusual arrangement of its rRNA genes, the 16S rRNA gene being separated from a 23S-5S rRNA cluster. We show that RNase III also initiates processing in this organism, by cleaving two typical stem structures encompassing 16S and 23S rRNAs and an atypical stem-loop located upstream of the 5S rRNA. Deletion of RNase III leads to the accumulation of a large 23S-5S precursor that is found in polysomes, suggesting that it can function in translation. Finally, we characterize a cis-encoded antisense RNA overlapping the leader of the 23S-5S rRNA precursor. We present evidence that this antisense RNA interacts with this precursor, forming an intermolecular complex that is cleaved by RNase III. This pairing induces additional specific cleavages of the rRNA precursor coupled with a rapid degradation of the antisense RNA.
Topics: Escherichia coli; Helicobacter pylori; Humans; Nucleic Acid Conformation; Oligonucleotides; Polyribosomes; RNA Precursors; RNA, Antisense; RNA, Bacterial; RNA, Ribosomal; RNA, Ribosomal, 16S; RNA, Ribosomal, 23S; RNA, Ribosomal, 5S; Ribonuclease III; Stomach Diseases
PubMed: 31006803
DOI: 10.1093/nar/gkz258 -
The Journal of Cell Biology Jun 1985Lysosomal enzymes have been shown to be synthesized as microsomal precursors, which are processed to mature enzymes located in lysosomes. We examined the effect of... (Comparative Study)
Comparative Study
Lysosomal enzymes have been shown to be synthesized as microsomal precursors, which are processed to mature enzymes located in lysosomes. We examined the effect of ammonium chloride on the intracellular processing and secretion of two lysosomal enzymes, beta-glucuronidase and beta-galactosidase, in mouse macrophages. This lysosomotropic drug caused extensive secretion of both precursor and mature enzyme forms within a few hours, as documented by pulse radiolabeling and molecular weight analysis. The normal intracellular route for processing and secretion of precursor enzyme was altered in treated cells. A small percentage of each precursor was delivered to the lysosomal organelle slowly. Most precursor forms traversed the Golgi apparatus, underwent further processing of carbohydrate moieties, and were then secreted in a manner similar to secretory proteins. The lag time for secretion of newly synthesized beta-galactosidase precursor was notably longer than that for the beta-glucuronidase precursor. The source of the secreted mature enzyme was the lysosomal organelle. Macrophages from the pale ear mutant were markedly deficient in secretion of mature lysosomal enzyme but secreted precursor forms normally. These results suggest that ammonia-treated macrophages contain two distinct intracellular pathways for secretion of lysosomal enzymes and that a specific block in the release of lysosomal contents occurs in the pale ear mutant.
Topics: Ammonium Chloride; Animals; Female; Galactosidases; Glucuronidase; Kinetics; Lysosomes; Macrophages; Mice; Mice, Inbred C57BL; Mice, Mutant Strains; Molecular Weight; Mutation; Protein Precursors; Subcellular Fractions; beta-Galactosidase
PubMed: 3922995
DOI: 10.1083/jcb.100.6.1894 -
The Biochemical Journal Sep 1983A procedure is described that allows the characterization of the molecular forms of beta-hexosaminidase and cathepsin D in controls and pathological specimens of human...
A procedure is described that allows the characterization of the molecular forms of beta-hexosaminidase and cathepsin D in controls and pathological specimens of human serum and human urine. The following observations were made. (1) In human serum, beta-hexosaminidase (alpha- and beta-chain) and cathepsin D are present predominantly in their high-molecular-weight precursor forms. In human urine, these enzymes exist as both precursor and mature forms. (2) Cathepsin D precursor from serum and urine differs in the number of oligosaccharides that are sensitive to endo-beta-N-acetylglucosaminidase H. Therefore the urine enzyme is not likely to originate from the serum. (3) The presence exclusively of precursors of beta-hexosaminidase and of cathepsin D in the sera of patients with hepatitis suggests that in hepatitis secretion of lysosomal enzymes is elevated, rather than the enzymes leaking from damaged cells. (4) In the urine of patients with nephrotic syndrome, beta-hexosaminidase and cathepsin D are present in grossly elevated amounts, but do not differ in the polypeptide patterns from controls. (5) In urine from a patient with mucolipidosis II, the elevated activity of beta-hexosaminidase is accounted for mainly by the precursor forms. Mature beta-chain of beta-hexosaminidase is lacking, and incompletely processed beta-hexosaminidase polypeptides are present. Both the precursor and the mature forms of cathepsin D are increased. They contain only complex oligosaccharides.
Topics: Cathepsin D; Cathepsins; Electrophoresis, Polyacrylamide Gel; Enzyme Precursors; Hexosaminidases; Humans; Liver; Liver Diseases; Lysosomes; Mucolipidoses; Nephrotic Syndrome; beta-N-Acetylhexosaminidases
PubMed: 6225425
DOI: 10.1042/bj2130733 -
Materials (Basel, Switzerland) Feb 2024Aluminum foam is a lightweight material and has excellent shock-absorbing properties. Various properties of aluminum foam can be obtained by changing the base aluminum...
Aluminum foam is a lightweight material and has excellent shock-absorbing properties. Various properties of aluminum foam can be obtained by changing the base aluminum alloy. Multi-layer aluminum foam can be fabricated by varying the alloy type of the base aluminum alloy, but with different foaming temperatures, within a single aluminum foam to achieve multiple properties. In this study, we attempted to fabricate a two-layer aluminum foam with the upper layer of a commercially pure aluminum A1050 foam and the lower layer of an Al-Si-Cu aluminum alloy ADC12 foam by using an optical heating device that can heat from both the upper and lower sides. Two types of heating methods were investigated. One is to directly stack the A1050 precursor coated with black toner on top of the ADC12 precursor and to foam it from the top and bottom by optical heating. The other is to place a wire mesh between the ADC12 precursor and the A1050 precursor and place the A1050 precursor on the wire mesh, thereby creating a space between the precursors, which is then foamed by optical heating from the top and bottom. It was shown that both precursors can be foamed and joined, and a two-layer A1050/ADC12 foam can be fabricated for both types of heating methods. In the method in which two precursors were stacked and foamed, even if the light intensity of the halogen lamps on the top and bottom were adjusted, heat conduction occurred between the stacked precursors, and the foaming of each precursor could not be controlled, resulting in tilting of the joining interface. In the method of foaming using a wire mesh with a gap between two precursors, it was found that by adjusting the light intensity, the two precursors can be foamed almost simultaneously and achieve similar pore structures. The joining interface can also be maintained horizontally.
PubMed: 38399143
DOI: 10.3390/ma17040894 -
Molecular and Cellular Biology Nov 1996The cytosolic heat shock cognate 70-kDa protein (hsc70) is required for efficient import of ornithine transcarbamylase precursor (pOTC) into rat liver mitochondria (K....
The cytosolic heat shock cognate 70-kDa protein (hsc70) is required for efficient import of ornithine transcarbamylase precursor (pOTC) into rat liver mitochondria (K. Terada, K. Ohtsuka, N. Imamoto, Y. Yoneda, and M. Mori, Mol. Cell. Biol. 15:3708-3713, 1995). The requirement of hsc70 for mitochondrial import of various precursor proteins and truncated pOTCs was studied by using an in vitro translation import system in which hsc70 was completely depleted. hsc70-dependent import of pOTC was about 60% of the total import, while import of the aspartate aminotransferase precursor, the serine:pyruvate aminotransferase precursor, and 3-oxoacyl coenzyme A thiolase was about 50, 30, and 0%, respectively. The subunit sizes of these four precursor proteins were 40 to 47 kDa. When pOTC was serially truncated from the COOH terminal, the hsc70 requirement decreased gradually and was not evident for the shortest truncated pOTCs of 90 and 72 residues. These truncated pOTCs were imported and proteolytically processed rapidly in 0.5 to 2 min at 25 degrees C, and the processed mature portions and the presequence portion were rapidly degraded. Sucrose gradient centrifugation analysis followed by import assay showed that pOTC synthesized in rabbit reticulocyte lysate forms an import-competent complex of about 11S in an hsc70-dependent manner. S values of import-competent forms of aspartate aminotransferase precursor, serine:pyruvate aminotransferase precursor, and 3-oxoacyl coenzyme A thiolase were 9S, 9S, and 4S, respectively. Thus, the S value decreased as the hsc70 dependency decreased. Precursor proteins were coimmunoprecipitated from the reticulocyte lysate containing the newly synthesized precursor proteins with an hsc70 antibody. The amount of coimmunoprecipitated proteins was much larger in the absence of ATP than in its presence. Among the four precursor proteins, the amount of coimmunoprecipitated protein decreased as the hsc70 dependency decreased.
Topics: Acetyl-CoA C-Acyltransferase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Cattle; DNA-Directed RNA Polymerases; Enzyme Precursors; HSP70 Heat-Shock Proteins; Kinetics; Macromolecular Substances; Mitochondria, Liver; Ornithine Carbamoyltransferase; Protein Biosynthesis; Protein Processing, Post-Translational; Rabbits; Rats; Reticulocytes; Transcription, Genetic
PubMed: 8887640
DOI: 10.1128/MCB.16.11.6103