Article Abstract:
Research was conducted to test the hypothesis that alkane hydroxylase from Acinetobacter sp strain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases. The alkM and its regulatory gene, alkR, have a completely different genetic organization from the arrangement found in P oleovorans. The similarity of AlkR to AraC-XylS-like transcriptional regulators suggests that the ADDP1 possess a different mechanism for the regulation of alkane utilization. Results also indicate that alkane degradation is not uniform in different strains.
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Article Abstract:
Acinetobacter calcoaceticus ADP1 contains two genes which produce rubredoxin and rubredoxin reductase which help the bacteria grow on dodecane. A mutant unable to grow on dodecane was complemented with an insert containing DNA from the wild strain containing two genes. One of the genes encodes for a rubredoxin similar to proteins produced by gram-positive bacteria and the other gene encoded a rubredoxin reductase similar to that produced by Pseudomonas oleovorans. If the rubredoxin encoding gene is disrupted by an insert the bacteria loses its ability of growing on dodecane.
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Article Abstract:
Phosphate starvation induces the transcription of polyphosphate kinase, suggesting that the ppk gene is involved in phosphorus metabolism. The ppk gene was isolated and cloned from Acinetobacter sp. strain ADP1. It encodes a putative polypeptide of 78.6 kDa with extensive homology to polyphosphate kinase from Escherichia coli and other bacteria. Phosphate starvation is found to trigger beta-galactosidase activity expressed from the single-copy ppk::lacZ fusion by 5- to 15-fold.
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