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Your search keyword '"Kuroda, Kouichi"' showing total 231 results
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231 results on '"Kuroda, Kouichi"'

39. Additional file 1 of Efficient ammonia production from food by-products by engineered Escherichia coli

Author

Tatemichi, Yuki, Kuroda, Kouichi, Takeharu Nakahara, and Ueda, Mitsuyoshi

Abstract

Additional file 1: Table S1. Concentration of glucose in various medium. Table S2. Primers used in this study. Table S3. Concentration of amino acids in various medium (expressed as mM). Figure S1. M9-yeast extract medium supplemented with (A) blank, (B) 10 mM glucose, or (C) 50 mM glucose was incubated by E. coli DH10B for 1–26.5 hours, and the amino acid concentrations were compared. Values are given as mean ± SD (n = 3).

Published
2020
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42. Additional file 4: of Temporal proteome dynamics of Clostridium cellulovorans cultured with major plant cell wall polysaccharides

Author

Aburaya, Shunsuke, Aoki, Wataru, Kuroda, Kouichi, Minakuchi, Hiroshi, and Ueda, Mitsuyoshi

Subjects
carbohydrates (lipids), sense organs, skin and connective tissue diseases
Abstract

Pathway analysis of glycolysis. Glycolysis pathway was constructed from KEGG. White box indicates the fold change of each protein relative to glucose at the same time point, and gray box indicates temporal profile of each protein relative to TP1 in each carbon sources. Each line indicates fold change or temporal profile (cellulose, red; xylan, purple; green, galactomannan; pectin, blue) (PDF 563 kb)

Published
2019
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43. Additional file 6: of Temporal proteome dynamics of Clostridium cellulovorans cultured with major plant cell wall polysaccharides

Author

Aburaya, Shunsuke, Aoki, Wataru, Kuroda, Kouichi, Minakuchi, Hiroshi, and Ueda, Mitsuyoshi

Subjects
skin and connective tissue diseases
Abstract

Pathway analysis of tricarboxylic acid cycle. Tricarboxylic acid cycle was constructed from KEGG. White box indicates the fold change of each protein relative to glucose at the same time point, and gray box indicates temporal profile of each protein relative to TP1 in each carbon source. Each line indicates fold change or temporal profile (cellulose, red; xylan, purple; galactomannan, green; pectin, blue) (PDF 708 kb)

Published
2019
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44. Additional file 7: of Temporal proteome dynamics of Clostridium cellulovorans cultured with major plant cell wall polysaccharides

Author

Aburaya, Shunsuke, Aoki, Wataru, Kuroda, Kouichi, Minakuchi, Hiroshi, and Ueda, Mitsuyoshi

Subjects
carbohydrates (lipids), animal structures, food and beverages, macromolecular substances, skin and connective tissue diseases
Abstract

Pathway analysis of xylan degradation and metabolism. Pathway of xylan degradation and metabolism was constructed from KEGG. White box indicates the fold change of each protein relative to glucose at the same time point, and gray box indicates temporal profile of each protein relative to TP1 in each carbon source. Each line indicates fold change or temporal profile (cellulose, red; xylan, purple; galactomannan, green; pectin, blue) (PDF 344 kb)

Published
2019
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45. Additional file 8: of Temporal proteome dynamics of Clostridium cellulovorans cultured with major plant cell wall polysaccharides

Author

Aburaya, Shunsuke, Aoki, Wataru, Kuroda, Kouichi, Minakuchi, Hiroshi, and Ueda, Mitsuyoshi

Subjects
carbohydrates (lipids), skin and connective tissue diseases
Abstract

Pathway analysis of galactomannan degradation and metabolism. (a) Pathway of mannan degradation and metabolism; (b) galactose degradation and metabolism pathway A. Each pathway was constructed from KEGG. White box indicates the fold change of each protein relative to glucose at the same time point, and gray box indicates temporal profile of each protein relative to TP1 in each carbon source. Each line indicates fold change or temporal profile (cellulose, red; xylan, purple; galactomannan, green; pectin, blue) (PDF 699 kb)

Published
2019
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46. Additional file 9: of Temporal proteome dynamics of Clostridium cellulovorans cultured with major plant cell wall polysaccharides

Author

Aburaya, Shunsuke, Aoki, Wataru, Kuroda, Kouichi, Minakuchi, Hiroshi, and Ueda, Mitsuyoshi

Subjects
carbohydrates (lipids), animal structures, food and beverages, macromolecular substances, skin and connective tissue diseases
Abstract

Pathway analysis of pectin degradation and metabolism. Pathway of pectin degradation and metabolism was constructed from KEGG. White box indicates the fold change of each protein relative to glucose at the same time point, and gray box indicates temporal profile of each protein relative to TP1 in each carbon source. Each line indicates fold change or temporal profile (cellulose, red; xylan, purple; galactomannan, green; pectin, blue) (PDF 656 kb)

Published
2019
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47. Development of a mito-CRISPR system for generating mitochondrial DNA-deleted strain in Saccharomyces cerevisiae.

Author

Amai, Takamitsu, Tsuji, Tomoka, Ueda, Mitsuyoshi, and Kuroda, Kouichi

Subjects
SACCHAROMYCES cerevisiae, MITOCHONDRIA, MITOCHONDRIAL DNA, DELETION mutation, PLANT mitochondria, YEAST, ETHIDIUM
Abstract

Mitochondrial dysfunction can occur in a variety of ways, most often due to the deletion or mutation of mitochondrial DNA (mtDNA). The easy generation of yeasts with mtDNA deletion is attractive for analyzing the functions of the mtDNA gene. Treatment of yeasts with ethidium bromide is a well-known method for generating ρ° cells with complete deletion of mtDNA from Saccharomyces cerevisiae. However, the mutagenic effects of ethidium bromide on the nuclear genome cannot be excluded. In this study, we developed a "mito-CRISPR system" that specifically generates ρ° cells of yeasts. This system enabled the specific cleavage of mtDNA by introducing Cas9 fused with the mitochondrial target sequence at the N-terminus and guide RNA into mitochondria, resulting in the specific generation of ρ° cells in yeasts. The mito-CRISPR system provides a concise technology for deleting mtDNA in yeasts. [ABSTRACT FROM AUTHOR]

Published
2021
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48. Construction of recombinant Escherichia coliproducing nitrogenase-related proteins from Azotobacter vinelandii

Author

Tatemichi, Yuki, Nakahara, Takeharu, Ueda, Mitsuyoshi, and Kuroda, Kouichi

Abstract

Biological nitrogen fixation by nitrogenase has attracted attention as an alternative method to chemical nitrogen fixation, which requires large amounts of fossil fuels. Azotobacter vinelandii, which produces an oxygen-sensitive nitrogenase, can fix nitrogen even under aerobic conditions; therefore, the heterologous expression of nif-related genes from A. vinelandiiis a promising strategy for developing a biological nitrogen fixation method. We assembled 17 nif-related genes, which are scattered throughout the genome of A. vinelandii, into synthetic gene clusters by overlap-extension-PCR and seamless cloning and expressed them in Escherichia coli. The transcription and translation of the 17 nif-related genes were evaluated by RT-qPCR and LC-MS/MS, respectively. The constructed E. colishowed nitrogenase activity under anaerobic and microaerobic conditions. This strain would be a useful model for examining the effect of other genes from A. vinelandiion nitrogen fixation by expressing them in addition to the minimal set of nif-related genes.Graphical AbstractAssembly of 17 nif-related genes into plasmids and expression in E. coli.

Published
2021
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