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Your search keyword '"Akimoto C"' showing total 2 results
Start Over Author "Akimoto C" Publisher oxford university press
2 results on '"Akimoto C"'

1. Cloning and characterization of cDNAs for the jasmonic acid-responsive Genes RRJ1 and RRJ2 in suspension-cultured rice cells.

Author

Sugimori M, Kiribuchi K, Akimoto C, Yamaguchi T, Minami E, Shibuya N, Sobajima H, Cho EM, Kobashi N, Nojiri H, Omori T, Nishiyama M, and Yamane H

Subjects
Blotting, Northern, Cells, Cultured, DNA, Complementary, Open Reading Frames, Oryza cytology, Oxylipins, Cyclopentanes pharmacology, Genes, Plant, Oryza genetics
Abstract

Two cDNA clones for jasmonic acid (JA)-responsive genes, RRJ1 and RRJ2, were isolated by differential screening from suspension-cultured rice cells treated with JA for 2 h. The putative RRJ1 protein is completely identical to that of a putative rice cystathionine gamma-lyase, while the putative RRJ2 protein is highly similar in sequence to a rice pyruvate decarboxylase, PDC1.

Published
2002
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2. Effects of the Escherichia coli sfsA gene on mal genes expression and a DNA binding activity of SfsA.

Author

Takeda K, Akimoto C, and Kawamukai M

Subjects
Amino Acid Sequence, Bacterial Proteins isolation & purification, Bacterial Proteins metabolism, DNA, Bacterial metabolism, DNA-Binding Proteins isolation & purification, DNA-Binding Proteins metabolism, Electrophoresis, Polyacrylamide Gel, Fermentation, Gene Expression Regulation, Molecular Sequence Data, Promoter Regions, Genetic genetics, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Bacterial Proteins genetics, DNA-Binding Proteins genetics, Escherichia coli genetics, Escherichia coli metabolism, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Genes, Bacterial, Maltose metabolism
Abstract

The sfsA gene was identified as one of the sfs genes the over-expression of which stimulates maltose fermentation of the Mal- Escherichia coli strain MK2001 (crp*1, cya:Km(r)). Expression from the malPQ promoter, which was measured using a chromosomally integrated malPp-lacZ fusion, was induced by over-expressing the sfsA gene in the crp*1, cya:Km(r) strain. The level of the MalE protein was increased in crp*1, cya:Km(r) cells over-producing SfsA. The SfsA protein was purified to homogeneity and tested for DNA binding activity. The purified SfsA protein binds to DNA non-specifically. All these results may suggest that SfsA functions as a DNA binding protein to induce the mal genes in coordination with CRP*1.

Published
2001
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