• Journal of Microbiology and Biotechnology
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• v.7 no.5
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• pp.341-344
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• 1997

Batch cultures of Anacystis nidulans BD-1 resistant to azaleucine and fluorotyrosine produced and liberated a wide range of amino acids, notably glutamic acid, alanine, phenylalanine, leucine, isoleucine, cysteine and methionine. Sustained liberation for prolonged periods was achieved after immobilization on calcium alginate and the net concentration in the medium was 0.18-0.2 g $I^{-1}$. While acetohydroxy acid synthase in azaleucine-resistant mutant lost leucine- and isoleucine-sensitivity, fluorotyrosine-resistant strain turned phenylalanine activating. The activities of nitrate assimilating enzymes were also higher in the mutants and were relaxed from ammonium-repression. The metabolic adjustments involved in amino acid overproduction are discussed.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1211-1216
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• 2004

A MNNG (N-methyl-N'-nitro-N-nitrosoguanidine) induced chromium resistant strain ($Cr^{r}18$) of unicellular cyanobacterium Anacystis nidulans has been isolated and characterized. The resistant strain could grow (although restricted to $50\%$ of control) in chromium concentration (180${\mu}M$) lethal to the wild-type. Sublethal ($160{\mu}M$) concentration of $Cr^{6+}$ significantly reduced (13-$37.5$) all the photosynthetic pigments of A. nidulans with maximum reduction in phycoerythrin followed by ChI $\alpha$. Pigments of A. nidulans were drastically decreased in lethal concentration of Cr^{6+} with maximum reduction in phycoerythrin ($75\%$) and allophycocyanin ($67.5\%$). Resistant strain $Cr^{r}18$ resisted toxic effects of sublethal and lethal concentrations of $Cr^{6+}$ on photosynthetic pigments as revealed by less decrease in pigments as compared to A. nidulans. Effect of $Cr^{6+}$ stress was also studied on nitrogen assimilation and phosphate uptake. Sublethal concentration of $Cr^{6+}$ drastically reduced ($71.5\%$) nitrate uptake by A. nidulans while a decrease of $29\%$ was observed in strain $Cr^{r}18$. Short (2 day) exposure of A. nidulans and its resistant strain $Cr^{r}18\;to\;Cr^{6+}$ did not affect nitrate reductase and glutamine synthetase (transferase), whereas longer (10 day) exposure to $Cr^{6+}$ lowered activities of both enzymes in A. nidulans but not significantly in the strain $Cr^{r}18$. Ammonium uptake by both strains was not affected by $Cr^{6+}$. Thus, $Cr^{6+}$ affected photosynthetic pigments, nitrogen assimilation, and phosphate uptake of A. nidulans, while strain $Cr^{r}18$ was able to resist toxic effects of the metal. Advantages of using strain $Cr^{r}18$ for bioremediation purposes have been evaluated by studying $Cr^{6+}$ removal from the solution. Resistant strain $Cr^{r}18$ was able to remove $33\%$ more $Cr^{6+}$ than A. nidulans and thus it can prove to be a good candidate for bioremediation of $Cr^{6+}$ from polluted waters.

• Journal of Plant Biology
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• v.38 no.1
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• pp.1-10
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• 1995

Photoinhibition and its recovery of spectrally adapted Anacystis nidulans were studied. Phycocyanin and Chl content and phycocyanin/Chl ratio were increased in cells grown under blue-green light compared with those grown in white light. Photosynthetic activities of white light and blue-green light grown cells were reduced by 50% after 15 min and 10 min of photoinhibitory light treatment (1.2 mmol·m-2s-1), respectively, largely due to the decline of PSII activities. However, their activities were recovered fully after 30 min incubation under weak light. Treatment of rifampicin and chloramphenicol magnified the photoinhibitory effects and suppressed the recovery with disappearance of susceptibility to photoinhibition and delayed the recovery process, indicating no significant differences in phosphorylation, dephosphorylation and protease activity between two cells. Therefore, it is suggested that the increased sensitivity of blue-green adapted cells might be attributed to the decline of protein synthesis, and phosphorylation-dephosphorylation of protein and protease activity might be involved in the recovery process.

• Korean Journal of Weed Science
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• v.13 no.2
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• pp.81-88
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• 1993

For searching the photosynthetic electron transport(PET) inhibitors, bio-rational screening system using thylakoid membranes extracted from wild and mutant cyanobacteria(Anacystis nidulans $R_2$) was developed. Generally, thylakoid membrane was more sensitive to the tested herbicides than the chloroplast from spinach in the Hill reaction. Higher resistant characteristics appeared in mutant D-5, Di-22 to diuron and mutant G-264 to atrazine as compared to wild type. To test the reaction of thylakoid membrane to herbicides, diuron and atrazine were applied simultaneously. Diuron and atrazine competed each other for binding with substituted amino acids, while diuron and dinoseb were non-competitive, and inhibiting activity was increased. Conclusively, bio-rational screening system using cyanobacteria was proved to be fast and efficient screening method for the development of PET inhibitors.

• Korean Journal of Weed Science
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• v.13 no.2
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• pp.89-95
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• 1993

The Inhibiting activity of newly synthesized phenol (E-series) and triazine (T-series) derivatives was evaluated by using thylakoid membranes extracted from cyanobacteria (Anacystis nidulans $R_2$). There were no significant differences between phenol derivatives and dinoseb to the thylakoid membrane extracted from wild type in the Hill reaction. However, a phenol derivative, E-24 which has no -Cl at phenyl ring, did not show any activity. The longer the length of R substituents was in phenol derivatives, the lower inhibiting activity was in the Hill reaction. Triazine derivatives, T-27, T-28, T-40, T-41, T-47 and T-48 were also compared with diuron and atrazine. Among triazine compounds, T-27 and T-28 showed 10 and 30 times activity as high as atrazine to wild type, respectively. Other triazine derivatives, T-40, T-41, T-47 and T-48 showed low inhibiting activity to wild and mutant type. A structural difference of T-27 and T-28 from T-40, T-41, T-47 and T-48 was the presented of -C-NH-. Both T-27 and T-28 were very closely associated with serine, an amino acid located at the 264th position of D1 protein because of the resistant ratio(R/S) to mutant G-264 were higher than that of atrazine.