Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and selected mutants

2003 ◽  
Vol 180 (6) ◽  
pp. 471-483 ◽  
Author(s):  
Naeima Yousef ◽  
Elfriede K. Pistorius ◽  
Klaus-Peter Michel
2010 ◽  
Vol 76 (10) ◽  
pp. 3153-3159 ◽  
Author(s):  
Eiji Suzuki ◽  
Hajime Ohkawa ◽  
Katsuya Moriya ◽  
Tatsuya Matsubara ◽  
Yukari Nagaike ◽  
...  

ABSTRACT ADP-glucose pyrophosphorylase (AGPase) and glycogen synthase (GS) catalyze the first two reactions of glycogen synthesis in cyanobacteria. Mutants defective in each of these enzymes in Synechococcus elongatus PCC 7942 were constructed and characterized. Activities of the corresponding enzymes in the selected mutants were virtually undetectable, and their ability to synthesize glycogen was entirely abolished. The maximal activities of photosynthetic O2 evolution and the rates of respiration in the dark were significantly decreased in the mutants compared to those in wild-type cells. Addition of 0.2 M NaCl or 3 mM H2O2 to liquid cultures markedly inhibited the growth of the AGPase and GS mutants, while the same treatment had only marginal effects on the wild type. These results suggest a significant role for storage polysaccharides in tolerance to salt or oxidative stress.


PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e59861 ◽  
Author(s):  
Jared M. Fraser ◽  
Sarah E. Tulk ◽  
Jennifer A. Jeans ◽  
Douglas A. Campbell ◽  
Thomas S. Bibby ◽  
...  

2008 ◽  
Vol 147 (2) ◽  
pp. 747-763 ◽  
Author(s):  
Anke Nodop ◽  
Daniel Pietsch ◽  
Ralf Höcker ◽  
Anke Becker ◽  
Elfriede K. Pistorius ◽  
...  

2009 ◽  
Vol 191 (15) ◽  
pp. 4863-4869 ◽  
Author(s):  
Javier Espinosa ◽  
Miguel Angel Castells ◽  
Karim Boumediene Laichoubi ◽  
Asunción Contreras

ABSTRACT The PII proteins are found in all three domains of life as key integrators of signals reflecting the balance of nitrogen and carbon. Genetic inactivation of PII proteins is typically associated with severe growth defects or death. However, the molecular basis of these defects depends on the specific functions of the proteins with which PII proteins interact to regulate nitrogen metabolism in different organisms. In Synechococcus elongatus PCC 7942, where PII forms complexes with the NtcA coactivator PipX, attempts to engineer PII-deficient strains failed in a wild-type background but were successful in pipX null mutants. Consistent with the idea that PII is essential to counteract the activity of PipX, four different spontaneous mutations in the pipX gene were found in cultures in which glnB had been genetically inactivated.


2006 ◽  
Vol 188 (14) ◽  
pp. 5258-5265 ◽  
Author(s):  
Roxane Lahmi ◽  
Eleonora Sendersky ◽  
Alexander Perelman ◽  
Martin Hagemann ◽  
Karl Forchhammer ◽  
...  

ABSTRACT Degradation of the cyanobacterial light-harvesting antenna, the phycobilisome, is a general acclimation response that is observed under various stress conditions. In this study we identified a novel mutant of Synechococcus elongatus PCC 7942 that exhibits impaired phycobilisome degradation specifically during nitrogen starvation, unlike previously described mutants, which exhibit aberrant degradation under nitrogen, sulfur, and phosphorus starvation conditions. The phenotype of the new mutant, AldΩ, results from inactivation of ald (encoding alanine dehydrogenase). AldΩ is deficient in transcription induction of a number of genes during nitrogen starvation. These genes include the “general nutrient stress-related” genes, nblA and nblC, the products of which are essential for phycobilisome degradation. Furthermore, transcripts of several specific nitrogen-responsive genes accumulate at lower levels in AldΩ than in the wild-type strain. In contrast, ald inactivation did not decrease the accumulation of transcripts during sulfur starvation. Transcription of ald is induced upon nitrogen starvation, which is consistent with the ability of wild-type cells to maintain a low cellular content of alanine under these conditions. Unlike wild-type cells, AldΩ accumulates alanine upon nitrogen starvation. Our analyses suggest that alanine dehydrogenase activity is necessary for an adequate cellular response to nitrogen starvation. Decomposition of alanine may be required to provide a sufficient amount of ammonia. Furthermore, the accumulated alanine, or a related metabolite, may interfere with the cues that modulate acclimation during nitrogen starvation. Taken together, our results provide novel information regarding cellular responses to nitrogen starvation and suggest that mechanisms related to nitrogen-specific responses are involved in modulation of a general acclimation process.


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