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Dual regulation of catecholate siderophore biosynthesis in Azotobacter vinelandii by iron and oxidative stress

Article Abstract:

Research has been conducted on the catecholate siderophore biosynthesis. The isolation of the gene required for this biosynthesis has been carried out.

Author: Tindale, Anne E., Mehrotra, Manisha, Ottem, Derek, Page, William J.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
Analysis, Oxidation, Physiological, Physiological oxidation, Iron, Iron (Metal), Microbiological research

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Alginate formation in Azotobacter vinelandii UWD during stationary phase and the turnover of poly-beta-hydroxybutyrate

Article Abstract:

Research to determine the role of RpoS in poly-beta-hydroxybutyrate. (PHB) turnover and alginate biosynthesis in Azotobacter vinelandii UWD during stationary phase has been carried out. A. vinelandii UWD is a mutant of strain UW defective in the respiratory oxidation of NADH. A. vinelandii strain UWD has been studied as a candidate for commercial production of polyhydroxyalkanoates (PHAs). They can be used as natural biodegradable plastics. The RpoD promoter possible isrecognized by the stationary phase sigma factor (RpoS), which may mediate alginate production in strain UWD.

Author: Page, William J., Tindale, anne, Chandra, Mark, Kwon, Elena
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2001
Physiological aspects, Gene mutations, Gene mutation, Plastics, Cytochemistry, Biodegradable plastics

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The Azotobacter vinelandii gene algJ encodes an outer-membrane protein presumably involved in export of alginate

Article Abstract:

The algJ gene from Azotobacter vinelandii was cloned utilizing a labelled RNA probe representing the coding region of the algE gene from Pseudomonas aeruginosa. The derived amino acid sequence of AlgJ was 52% identical with AlgE from P. aeruginosa. The hydrophilicity profile and the amphipathicity of regions in the amino acid sequence of AlgJ were very close to AlgE. A topological model was developed where AlgJ was represented as a beta-barrel with 18 beta-strands inserted in the outer membrane.

Author: Rehm, Bernd H.A.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
Membrane proteins, Pseudomonas aeruginosa

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Subjects list: Statistical Data Included, Research, Canada, Biosynthesis, Genetic aspects, Bacteria
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