Physiol Mol Biol Plants
March 2018
Unbranched heterocytous cyanobacteria produce a number of serine peptidases. We have characterized several peptidases in the cell-free extracts of a true-branched N-fixing cyanobacterium, sp. nov.
View Article and Find Full Text PDFNostoc is a complex and tough genus to differentiate, and its morphological plasticity makes it taxonomically complicated. Its cryptic diversity and almost no distinguishable morphological characteristics make this genus incredibly heterogeneous to evaluate on taxonomic scales. The strain NOS, isolated from a eutrophic water body, is being described as a new genus Aliinostoc with the strain showing motile hormogonia with gas vesicles as an atypical feature, which is currently considered as the diacritical feature of the genus but should be subjected to critical evaluation in the near future.
View Article and Find Full Text PDFA bentazone-resistant mutant of Synechococcus elongatus PCC7942, called Mu2, tolerated elevated NaCl concentrations. As bentazone and bromoxynil exhibit similar mechanism of action, we investigated whether the mutant also toleratedbromoxynil and found it to be true. The line of investigation was then whether the acclimation strategy for the three stressors, bentazone, bromoxynil and NaCl was same or different.
View Article and Find Full Text PDFA unicyanobacterial isolate of cyanobacterium, identified as Microcystis Ku2, produced a mammalian elastase-inhibitory lipid derivative. Protease inhibitors in cyanobacteria are unequivocally peptides. Since this metabolite appeared in lipid phase, we worked on a hypothesis that whether metabolite other than peptides could be responsible for the characteristic inhibition.
View Article and Find Full Text PDFIn this article, we describe the modifications in the antioxidant system of Synechococcus elongatus PCC7942 mutant Mu2 capable of growing at five times higher concentration of bentazone than wild type. Nevertheless, in both the strains, bentazone almost identically induced light-dependent H(2)O(2) production and its extracellular release. However unlike the wild type, peroxide produced upon prolong bentazone incubation was immediately degraded in Mu2.
View Article and Find Full Text PDFMicrocystin synthetase-gene-specific primers were used to identify hepatotoxic microcystin producing genotypes in six Microcystis spp.-dominant water blooms. Four blooms gave positive PCR reaction.
View Article and Find Full Text PDFFollowing a N-methyl-N'-nitro-N-nitrosoguanidine-based mutagenesis of Synechococcus elongatus PCC 7942 wild type, we were able to select several mutants with an enhanced tolerance toward the herbicide bentazone (3-isopropyl-1H-2,1,3-benzothiadiazine-4(3H)-one 2,2-dioxide). Mutant Mu1 has in part been previously characterized. In the present paper we report on another mutant, called Mu2, which also has a higher tolerance toward bentazone.
View Article and Find Full Text PDFIn this article we describe the partial characterization of a Synechococcus sp. PCC 7942 mutant Mu1 with an enhanced resistance towards the herbicide bentazone (3-isopropyl-1H-2,1,3-benzothiadiazine-4(3H)-one 2,2-dioxide). The mutant was derived from a random mutagenesis with N-methyl-N'-nitro-N-nitrosoguanidine (NSG) and exhibited superior growth rates, pigment content and overall photosynthetic activities under regular growth conditions compared to wild type.
View Article and Find Full Text PDFMany cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D.
View Article and Find Full Text PDFThe paper describes the characterization of proteases in the whole body homogenate of Moina macrocopa, which can possibly be inhibited by the extracts of Microcystis aeruginosa PCC7806. With the use of oligopeptide substrates and specific inhibitors, we detected the activities of trypsin, chymotrypsin, elastase and cysteine protease. Cysteine protease, the predominant enzyme behind proteolysis of a natural substrate, casein, was partially purified by gel filtration.
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