Loss of allosteric control but retention of the bifunctional catalytic competence of a fusion protein formed by excision of 260 base pairs from the 3' terminus of pheA from Erwinia herbicola
Article Abstract:
The pheA gene of Erwinia herbicola codes for a P protein with chorismate mutase (CM-P) and prephenate dehydratase (PDT) activities. A truncated pheA gene, containing a deletion of 260 base pairs in the 3' terminus was expressed in Escherichia coli and its product was characterized. The results showed that the truncated protein retained both CM-P and PDT activities. However, the expression of the enzymes showed a loss of allosteric control. These results demonstrate that the deleted region represents a regulatory domain for the allosteric control of pheA expression.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Antibiotic production by Erwinia herbicola Eh1087: its role in inhibition of Erwinia amylovora and partial characterization of antibiotic biosynthesis genes
Article Abstract:
TnphoA mutagenesis was used to select 12 mutants of Eh1087 that failed to inhibit Erwinia amylovora in vitro to determine the role of antibiosis in Eh1087's control of disease. Antibiosis was found to play a critical role in the suppression of disease by strain Eh1087, with mutants in immature pear fruit Ant- growing at the same rate as Eh1087 but not suppressing development of the disease caused by E. amylovora. A 2.2-kb region of DNA showed tight clustering of TnphoA insertions.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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L-Arogenate is a chemoattractant which can be utilized as the sole source of carbon and nitrogen by Pseudomonas aeruginosa
Article Abstract:
Pseudomonas aeruginosa uses L-arogenate as a chemoattractant molecule, which is the only source of both carbon and nitrogen. Mutants that lack cyclohexadienyl dehydratase or phenylalanine hydroxylase have decreased growth rates during utilization of L-arogenate as nitrogen source. L-arogenate catabolism occurs through alternative pathways converging at 4-hydroxyphenylpyruvate.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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