the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
a truncated enzyme version, devoid of the phosphatase part, synthesizes glucosylglycerol-phosphate, in contrast to the full-length wild-type enzyme, that synthesizes glucosylglycerol. The complete GgpPS protein also catalyzes dephosphorylation of glucosylglycerol phosphate, overview
a truncated enzyme version, devoid of the phosphatase part, synthesizes glucosylglycerol-phosphate, in contrast to the full-length wild-type enzyme, that synthesizes glucosylglycerol. The complete GgpPS protein also catalyzes dephosphorylation of glucosylglycerol phosphate, overview
the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
GgpS is inhibited by nucleic acids in a sequence- and length-independent manner in vitro and in vivo, it binds DNA, RNA, and heparin via a salt-dependent electrostatic interaction with the negatively charged backbone of the polyanions. Non-competitive inhibition. The inhibition is completely abolished by 20 mM NaCl
GgpS is the key enzyme of the glucosylglycerol pathway The intermediate is dephosphorylated by the second enzyme of the pathway, the glucosylglycerol-phosphate phosphatase, GgpP
the enzyme is synthesized at a basal level under low salt conditions. It is largely inactive and is activated after a salt shock. Since the recombinant enzyme purified from Escherichia coli has NaCl-independent activity, it is concluded that an inhibitor bound to GgpS is removed by NaCl in vivo
the moderately halotolerant cyanobacterium Synechocystis sp. PCC 6803 synthesizes glucosylglycerol as a compatible solute. Mechanism of activity regulation by the nonspecific salt-dependent binding of an enzyme to nucleic acids, overview
construction of a truncated enzyme version devoid of the phosphatase part, which synthesizes glucosylglycerol-phosphate, in contrast to the full-length protein, that synthesizes glucosylglycerol, dephosphorylation of glucosylglycerol phosphate is detected only with the complete GgpPS protein, overview. Expression of the full-length ggpPS gene leads to complementation of the salt-sensitive phenotype of the mutant defective in the phosphatase step showing a severe drop in salt resistance because of the toxic effect of glucosylglycerol phosphate accumulation
construction of a truncated enzyme version devoid of the phosphatase part, which synthesizes glucosylglycerol-phosphate, in contrast to the full-length protein, that synthesizes glucosylglycerol, dephosphorylation of glucosylglycerol phosphate is detected only with the complete GgpPS protein, overview. Expression of the full-length ggpPS gene leads to complementation of the salt-sensitive phenotype of the mutant defective in the phosphatase step showing a severe drop in salt resistance because of the toxic effect of glucosylglycerol phosphate accumulation
gene ggpPS, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and truncated mutant enzymes in Escherichia coli strain LMG194, complementation of the glucosylglycerol-defective mutants of the cyanobacterium Synechocystis sp. strain PCC 6803
plasmid-bound expression of ggpS and ggpP from Synechocystis sp. PCC 6803 enables synthesis of alpha-D-glucosylglycerol exclusively in osmotically stressed cells of Corynebacterium glutamicum (pEKEx2-ggpSP), which is probably due to the unique intrinsic control mechanism of GG-phosphate synthase activity in response to intracellular ion concentrations
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ggpS mRNA shows a salt-dependent accumulation that roughly follows the kinetics of the intracellular salt ion concentrations in response to salt shocks. The induction of ggpS expression involves several regulatory components in Synechocystis
Hagemann, M.; Effmert, U.; Kerstan, T.; Schoor, A.; Erdmann, N.
Biochemical characterization of glucosylglycerol-phosphate synthase of Synechocystis sp. strain PCC 6803: Comparison of crude, purified, and recombinant enzymes
Salt-dependent expression of glucosylglycerol-phosphate synthase, involved in osmolyte synthesis in the cyanobacterium synechocystis sp. strain PCC 6803