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  • 1
    Electronic Resource
    Electronic Resource
    Release of glucosylglycerol from the cyanobacterium Synechocystis spec. SAG 92.79 by hypoosmotic shock (1990)
    Springer
    Archives of microbiology 153 (1990), S. 405-408 
    Details
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Exudation ; Salt stress ; Glucosylglycerol ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When cells of Synechocystis, adapted to 684 mmol/l NaCl, were exposed to hypoosmotic shock by reducing NaCl concentration to more than 250 mmol/l, significant amounts of organic material were liberated which could be increased by increasing shock strength. After maximal hypoosmotic shock (684 mmol/l→ 2 mmol/l NaCl) 40–50% of photosynthetically labelled organic material occurred in the surrounding medium. The main compound exudates was the osmoprotective compound glucosylglycerol. Minor exudates were amino acids, organic acids and carbohydrates. In contrast a hyperosmotic shock (2 mmol/l→684 mmol/l NaCl) liberated only one fourth of the amount liberated by a hypoosmotic shock.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249013
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of salt- and heat-induced alterations of protein synthesis in the cyanobacterium Synechocystis sp. PCC 6803 (1991)
    Springer
    Archives of microbiology 155 (1991), S. 587-592 
    Details
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Salt shock ; Heat shock ; Protein synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein synthesis of the cyanobacterium Synechocystis spec. PCC 6803 decreases after a 684 mM NaCl salt shock. Qualitative changes were observed during the shock and the subsequent adaptation process using one-dimensional polyacrylamide electrophoresis. Proteins of apparent molecular masses of 13.0, 14.2, 16.6, 20.0, 21.0, 23.0, 33.0, 47.0, 52.0, 65.0 and 72.0 kDa are synthesized at enhanced rates after salt stress. The proteins of 14.2, 21.1 and 52.0 kDa are transiently induced during the first hours of the adaptation phase, while the other proteins are also synthesized at enhanced rates in salt-adapted cells. The proteins of 14.2, 23.0, 33.0 and 65.0 kDa are also induced by heat shock (43°C). Heat shock proteins of about 88.0, 75.0, 58.0, 17.5 and 13.8 kDa, in contrast, are induced by heat shock but not by salt. Two-dimensional polyacrylamide electrophoresis showed that the induced salt and heat shock proteins in some cases consisted of isoforms of different isoelectric points.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245354
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  • 3
    Electronic Resource
    Electronic Resource
    Selection and characterization of mutants of the cyanobacterium Synechocystis sp. PCC 6803 unable to tolerate high salt concentrations (1992)
    Springer
    Archives of microbiology 158 (1992), S. 429-434 
    Details
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Glucosylglycerol ; Random cartridge mutagenesis ; Salt tolerance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three mutants of the cyanobacterium Synechocystis sp. PCC 6803 unable to tolerate high salt concentrations were generated using random cartridge mutagenesis. Analysis of the phenotypes revealed that the salt sensitivity of one mutant (6803/143) is caused by a block in the synthesis of the osmoprotective substance glucosylglycerol, while in the two other mutants no physiological defect could be detected which was responsible for the loss of salt tolerance. Southern hybridization analyses and cloning of the integration sites of the resistance marker demonstrated that different genes are affected in each of the three mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276304
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of salt-induced periplasmic proteins from Synechocystis sp. strain PCC 6803 (1999)
    Springer
    Archives of microbiology 171 (1999), S. 214-217 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cyanobacteria ; Periplasmic proteins ; Salt ; adaptation ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Periplasmic proteins were obtained from control cells and salt-adapted cells of the cyanobacterium Synechocystis sp. PCC 6803 using the method of cold osmotic shock. Two of these proteins (PP 1, apparent mol. mass 27.6 kDa, and PP 3, apparent mol. mass 39.9 kDa) were accumulated in high amounts in the periplasm of salt-adapted cells, while the major periplasmic protein (PP 2, apparent mol. mass 36.0 kDa) was accumulated independently from salt. After isolation from gels and partial sequencing, the proteins could be assigned to proteins deduced from the complete genome sequence of Synechocystis. Neither salt-induced periplasmic proteins (PP 1, Slr0924 and PP 3, Slr1485) exhibited sequence similarity to proteins of known function from databases. The major protein (PP 2-Slr0513) showed significant sequence similarities to iron-binding proteins. All proteins included typical leader sequences at their N-terminus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050702
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of glucosylglycerol in salt-stressed cells of the cyanobacterium Microcystis firma (1987)
    Springer
    Archives of microbiology 148 (1987), S. 275-279 
    Details
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Microcystis ; Glucosylglycerol ; Salt adaptation ; Synthesis rate ; Turnover
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The unicellular cyanobacterium Microcystis furma tolerates salinity by accumulating the osmoprotective compound glucosylglycerol. After salt shock, the initial rate of glucosylglycerol synthesis is independent of the NaCl concentration used. In pulse chase experiments with NaH14CO3, synthesis of glucosylglycerol by salt-adapted cells was found to be rapid, whereas no sign of its breakdown was detected. Therefore, it is concluded that no turnover of glucosylglycerol takes place in salt-adapted cells. The specific capacity of the glucosylglycerol-forming enzyme system may be one reason for the salt resistance limit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00456704
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  • 6
    Electronic Resource
    Electronic Resource
    Glucosylglycerol-phosphate synthase: target for ion-mediated regulation of osmolyte synthesis in the cyanobacterium Synechocystis sp. strain PCC 6803 (1999)
    Springer
    Archives of microbiology 171 (1999), S. 101-106 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cyanobacteria ; Glucosylglycerol-phosphate ; synthase/phosphatase ; Ions ; Osmolytes ; Salt activation ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The response of cyanobacteria to a changing osmotic environment includes the accumulation of organic osmolytes such as glucosylglycerol. The activation of the enzymes involved in glucosylglycerol synthesis [glucosylglycerol-phosphate synthase (GGPS) and glucosylglycerol-phosphate phosphatase (GGPP)] in Synechocystis sp. strain PCC 6803 by various salts and salt concentrations was investigated in vitro. GGPS seemed to be the target for salt-mediated regulation of glucosylglycerol synthesis in vitro. GGPS activation was dependent on the concentration of NaCl, and a sigmoidal plot was obtained. Sensitivity to NaCl was markedly enhanced by low Mg+2 concentrations (optimal at 4 mM), but Mg2+ was not absolutely necessary for the Na+ stimulation. As in the case of NaCl, other salts (including MgCl2) stimulated GGPS. The relative order of GGPS activation in the presence of chloride by the cations at constant ionic strength was Li+ 〉 Na+ 〉 K+, Mg2+ Mn2+. No absolute dependence on ionic strength was observed in Mg2+/Na+-exchange experiments. The degree of activation by ions at various concentrations was positively related to the increasing destabilizing properties of the cations according to the Hofmeister rule, where chaotropic cations are most efficient. Cations were responsible for activation since chaotropic anions counteracted the activating effect of cations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050684
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of a glucosylglycerol-phosphate-accumulating, salt-sensitive mutant of the cyanobacterium Synechocystis sp. strain PCC 6803 (1996)
    Springer
    Archives of microbiology 166 (1996), S. 83-91 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cyanobacteria ; Glucosylglycerol-phosphate ; Osmoprotective compounds ; Random ; cartridge mutagenesis ; Salt adaptation ; StpA protein ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Salt-sensitive mutants of Synechocystis were obtained by random cartridge mutagenesis, and one mutant (mutant 4) was characterized in detail. The salt tolerance of mutant 4 was reduced to about 20% of that of the wild-type. This was caused by a defect in the biosynthetic pathway of the osmoprotective compound glucosylglycerol (GG). Salt-treated cells of mutant 4 accumulated the intermediate glucosylglycerol-phosphate (GG-P). Only low levels of phosphate-free GG were detected. The phosphorylated form of GG was not osmoprotective and seemed to be toxic. In vitro enzyme assays revealed that GG-P-phosphatase activity was completely absent in mutant 4, while GG-P-synthase remained unchanged. The integration site of the aphII cartridge in mutant 4 and the corresponding wild-type region was cloned and sequenced. Mutant 4 was complemented to salt resistance after transformation by the cloned wild-type region. The integration of the cartridge led to a deletion of about 1.1 kb of the chromosomal DNA. This affected two of the identified putative protein coding regions, orfII and stpA. The ORFII protein shows a high degree of similarity to the receiver domain of response regulator proteins. Related sequences were not found for StpA. We assume that in mutant 4, regulatory genes necessary for the process of salt adaptation in Synechocystis are impaired.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050360
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  • 8
    Electronic Resource
    Electronic Resource
    Identification of salt-regulated genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 by subtractive RNA hybridization (1999)
    Springer
    Archives of microbiology 172 (1999), S. 377-386 
    Details
    ISSN: 1432-072X
    Keywords: Key words Chaperone ; Cyanobacteria ; groEL ; isiA ; RNA helicase ; Salt stress ; Subtractive RNA ¶hybridization ; Synechocystis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To identify genes transcribed preferentially under salt stress, a subtractive RNA hybridization procedure was applied to the cyanobacterium Synechocystis sp. PCC 6803. The screening of a genomic library led to the identification of several RNA species that were more abundant in salt-stressed cells than in control cells. Salt-dependent transcription of the identified genes was verified in Northern blot experiments. In addition to the previously characterized genes cpn60 (encoding GroEL; a molecular chaperone) and isiA (encoding a chlorophyll-binding protein), genes encoding a protein of unknown function (slr0082) and a putative RNA helicase (slr0083) were identified as salt-regulated genes in Synechocystis. Genes slr0082 and slr0083, located at sites adjacent to each other on the Synechocystis chromosome, were transcribed from separate promoters and showed the most significant induction 1–3 h after salt shock. The salt-regulated promoters of these two genes were mapped. Genes cpn60, slr0082, and slr0083 were also found to be induced by a cold shock. The possible role of the identified gene products for salt adaptation of Synechocystis is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050774
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