Abstract
Repression of alkaline phosphatase (APase) activity in four taxonomically different cyanobacteria Anabaena flosaquae, Calothrix brevissima, Scytonema javanicum and Hapalosiphon intricatus by rifampicin and chloramphenicol led to the conclusion that enzyme synthesis is under transcriptional control. A mutant isolated in Nostoc muscorum after mutagenesis with NTG was found to be defective in APase activity (APase def). The mutant showed nearly 90% growth compared to wild type strain in the presence of inorganic phosphate (Pi). The wild type Nostoc muscorum showed some growth (33% compared to Pi) in the presence of organic phosphate but the growth of the APase def mutant was negligible under these conditions since it lacks APase activity. APase activity and phosphate uptake functions were phosphate repressible in the wild type strain. Phosphate uptake in the mutant was comparable to the wild type cyanobacterium. The mutant was also able to accumulate polyphosphate granules like the wild type.
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Pandey, M., Tiwari, D. Characteristics of alkaline phosphatase in cyanobacterial strains and in an APase def mutant of Nostoc muscorum . World Journal of Microbiology and Biotechnology 19, 279–284 (2003). https://doi.org/10.1023/A:1023602208011
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DOI: https://doi.org/10.1023/A:1023602208011