Azide-resistant mutants in Acinetobacter calcoaceticus A2 are defective in protein secretion.
Azide, an inhibitor of ATPase, and a specific inhibitor of protein export was used in order to select for protein secretion mutants in Acinetobacter calcoaceticus A2. Two such mutants were isolated that were azide-resistant and defective in the general protein transport system. The mutation also conferred additional phenotypic changes, including an inability to grow on minimal media or at 40 degrees C. The existence of protein secretion mutants with a selectable phenotype may be useful for the genetic study of protein export.
Elkeles
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A
Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
Rosenberg
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E
Ron
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EZ
D016954:Acinetobacter calcoaceticus / Q000235:genetics / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000235:genetics; D000469:Alkaline Phosphatase / Q000378:metabolism; D001386:Azides / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003470:Culture Media; D004352:Drug Resistance, Microbial; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial / Q000235:genetics*; D026901:Membrane Transport Proteins; D016296:Mutagenesis; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D001618:beta-Lactamases / Q000378:metabolism
D001386:Azides; D001426:Bacterial Proteins; D003470:Culture Media; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D000469:Alkaline Phosphatase; D001618:beta-Lactamases; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins