Analysis of the Rhizobium leguminosarum siderophore-uptake gene fhuA:differential expression in free-living bacteria and nitrogen-fixing bacteriods and distribution of fhuA pseudogene in different strains

Article Abstract:

Results show that fhuA gene codes for a receptor for the siderophore and the gene itself is regulated by iron. Data also reveal that a pseudogene version is detected in some strains of the Rhizonium bacterium.

United Kingdom, United States, Statistical Data Included, Physiological aspects, Gene mutations, Gene mutation, Iron, Iron (Metal), Nitrogen, Pseudogenes, Nitrogen fixation

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High affinity iron acquisition in Rhizobium leguminosarum requires the cycHJKL operon and the feuPQ gene products, which belong to the family of two-component transcriptional regulators

Article Abstract:

Functional and genetic studies were done to characterize the cycHJKL operon and the feuPQ gene products which belong to the family of two-component transcriptional regulators. Mutational analysis of the cycHJKL gene revealed that the gene plays the role of maintaining bacteria's high affinity iron acquisition system that is important for their symbiotic nitrogen fixation. The genes feuP and feuQ which are located upstream of the cycH and lipA genes, on the other hand, were shown not to affect the transcription of either lipA or cyhHJKL operon. A mutation in feuQ, however, caused the loss of the high affinity iron uptake system.

Research, Analysis, Genetic transcription, Transcription (Genetics), Molecular microbiology

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The fhu genes of Rhizobium leguminosarum, specifying siderophore uptake proteins: fhuDCB are adjacent to a pseudogene version of fhuA

Article Abstract:

A mutant of Rhizobium leguminosarum, which cannot take up the siderophore vicibactin, was isolated. The mutation is in a homolog of fhuB, which in Escherichia coli, encodes an inner-membrane protein of the ferric hydroxamate uptake system. In Rhizobium, fhuB is an operon fhuDCB, which encodes the cytoplasmic membrane and periplasmic proteins required in siderophore uptake. The fhuDCB mutants produce vicibactin when grown in iron concentrations that suppress its production in the wild-type.

Bacterial proteins

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