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  • 1
    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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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Uptake and use of the osmoprotective compounds trehalose, glucosylglycerol, and sucrose by the cyanobacterium Synechocystis sp. PCC6803 (1997)
    Springer
    Archives of microbiology 167 (1997), S. 112-118 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cyanobacterium ; Synechocystis sp. ; Osmoregulation ; Salt adaptation ; Trehalose ; Glucosylglycerol ; Sucrose ; Sucrase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Accumulation of exogenously supplied osmoprotective compounds was analyzed in the cyanobacterium Synechocystis sp. PCC6803, which synthesizes glucosylglycerol as the principal osmoprotective compound. Glucosylglycerol and trehalose were accumulated to high levels and protected cells of a mutant unable to synthesize glucosylglycerol against the deleterious effects of salt stress. In the wild-type, uptake of trehalose repressed the synthesis of glucosylglycerol and caused metabolic conversion of originally accumulated glucosylglycerol. Trehalose cannot be synthesized by Synechocystis and was not or only insignificantly metabolized. Sucrose, which can be synthesized in low quantities by Synechocystis, was also taken up, as indicated by its disappearance from the medium. Sucrose was not accumulated to high levels, probably due to a sucrose-degrading activity found in cells adapted to both low- and high-salt conditions. Despite its low intracellular concentration, sucrose showed a weak osmoprotective effect in salt-shocked cells of a mutant unable to synthesize glucosylglycerol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050423
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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
    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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  • 6
    Electronic Resource
    Electronic Resource
    Salt-dependent protein phosphorylation in the cyanobacterium Synechocystis PCC 6803 (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 113 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Hyper- and hypo-osmotic salt shocks in the presence of [32P]PO43− led to the appearance and disappearance of several 32P-labelled proteins in vivo within a few minutes. Similar to the in vivo labelling experiments, a 20.5-kDa protein was also more intensely labelled in extracts from salt-shocked cells using [γ-32P]ATP in in vitro labelling experiments. Furthermore, labelling of this and a protein of about 64.4 kDa was induced by adding high amounts of NaCl directly to extracts of control cells in kinase assays. Therefore, changes in the NaCl contents led to alterations of the activity of protein in Synechocystis sp. PCC 6803, which may be involved in the signal transduction chain sensing changes in the NaCl content of the surrounding medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06515.x
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  • 7
    Electronic Resource
    Electronic Resource
    Salt effects on 77K fluorescence and photosynthesis in the cyanobacterium Synechocystis sp. PCC 6803 (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 71 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Salt loading of 314 mmol l−1 NaCl led to optimal growth and photosynthesis in Synechocystis sp. PCC 6803. In 77K fluorescence emission spectroscopy a new peak was found at 660 nm in salt adapted cells, in addition to the peaks of chlorophyll-a at fluorescence levels (F) 685 and 725 nm. Futhermore the ratios of F685/F725 and of photosystem 2/photosystem 1 are reduced in salt loaded cells in comparison to control cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb03817.x
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis of the compatible solutes glucosylglycerol and trehalose by salt-stressed cells of Stenotrophomonas strains (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 243 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In this study, physiological processes were analysed, which are involved in salt acclimation of two Stenotrophomonas species, Stenotrophomonas maltophilia strain DSM 50170 and Stenotrophomonas rhizophila strain DSM 14405. S. maltophilia accumulated trehalose as the only osmolyte, whereas S. rhizophila produced additionally to trehalose glucosylglycerol (GG). The different spectrum and amounts of compatible solutes in these two strains led to differences in terms of their salt tolerance. The human-associated S. maltophilia was able to grow in media containing up to 3% NaCl (w/v). In contrast, S. rhizophila propagated in salinities up to 5% NaCl (w/v). The strain was isolated from the rhizosphere, a microenvironment which is characterised by high and changing salinities. Light microscopic analysis of S. rhizophila cells showed a significant increase in cell length of salt-treated cells in comparison to control cells. Cells of S. rhizophila exposed to more than 2% NaCl excreted GG into the medium during the transition from exponential to stationary growth phase, while the internal trehalose pool remained constant. This feature offers a high potential for the biotechnological production of GG.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2004.12.005
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  • 9
    Electronic Resource
    Electronic Resource
    Repression by Fur is not the main mechanism controlling the iron-inducible isiAB operon in the cyanobacterium Synechocystis sp. PCC 6803 (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 227 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The iron deficiency-dependent regulation of isiAB transcription in Synechocystis sp. PCC 6803 was analyzed by fusion of modified isiAB promoter fragments to gfp and in vivo quantification of Gfp fluorescence. For the putative Fur box only a slight repressing impact on promoter activity could be shown. In a heteroallelic fur mutant a corresponding incomplete repression of isiAB transcription under iron-replete conditions confirmed the role of Fur in isiAB regulation. However, a 90 bp region upstream of the putative −35 box of the isiAB promoter was essential for full promoter activity under iron-deplete conditions. This pattern indicates a dual promoter regulation by both a repressing mechanism exhibited via the Fur system and an unknown activating mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00689-X
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  • 10
    Electronic Resource
    Electronic Resource
    The iron-regulated isiA gene of Fischerella muscicola strain PCC 73103 is linked to a likewise regulated gene encoding a Pcb-like chlorophyll-binding protein (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 197 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The expression of the chlorophyll a-binding, iron stress-induced protein IsiA is part of the cyanobacterial response to iron deficiency. A new isiA gene from the filamentous heterocystous cyanobacterial strain, Fischerella muscicola PCC 73103, was identified using standard and inverse PCR. While in unicellular cyanobacterial strains isiA is organized in an operon with isiB (encoding flavodoxin), in Fischerella not an isiB gene but another chlorophyll-binding protein encoding gene was identified downstream of isiA, which shows significant similarities to Pcb-like protein encoding genes known from prochlorophytes. The expression of both genes was clearly activated under iron deficiency. Although isiA and pcbC were independently transcribed, the size of the pcbC transcript indicates a large iron-regulated operon. Beside a 10-fold increase of isiA transcript content iron-starved cells of Fischerella showed a blue-shift in the red chlorophyll a absorption peak. In addition, chlorophyll fluorescence at 77 K was dominated by an emission peak at 685 nm. These features are in accordance with the characteristics of IsiA accumulation in iron-starved unicellular cyanobacteria, suggesting identical IsiA function in heterocystous strains in spite of different genetic organization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10593.x
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