Synechococcus sp. PCC7942 Transformed with Escherichia coli bet Genes Produces Glycine Betaine from Choline and Acquires Resistance to Salt Stress

Nomura, Masatoshi; Ishitani, Manabu; Takabe, Tetsuko; K., A.

doi:10.1104/pp.107.3.703

Cited by 115 publications

(64 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The plasmids pUC303-KatE (15), pUC303-Bet (13), and pUC303-KatE͞Bet (15) were used for the expression of mono-functional catalase, betaine, and both catalase and betaine, respectively. The plasmid pUC303-Bm was used in the control cells (13). For the construction of expression plasmid pUC303-DnaK, the 3-kbp fragment that contains the dnaK gene from A. halophytica (20) was digested with SspI and EcoRV and blunt-ended, and then ligated into the EcoRI-and SalI-double-digested and blunt-ended site of pUC303-Bm.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Waditee

Hibino

Nakamura

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

122

View full text Add to dashboard Cite

The salt tolerance of a freshwater cyanobacterium, Synechococcus sp. PCC 7942, transformed with genes involved in the synthesis of a Na ؉ ͞H ؉ antiporter, betaine, catalase, and a chaperone was examined. Compared with the expression of betaine, catalase, and the chaperone, the expression of the Na ؉ ͞H ؉ antiporter gene from a halotolerant cyanobacterium (ApNhaP) drastically improved the salt tolerance of the freshwater cyanobacterium. The Synechococcus cells expressing ApNhaP could grow in BG11 medium containing 0.5 M NaCl as well as in sea water, whereas those expressing betaine, catalase, and the chaperone could not grow under those conditions. The coexpression of ApNhaP with catalase or ApNhaP with catalase and betaine did not further enhance the salt tolerance of Synechococcus cells expressing ApNhaP alone when grown in BG11 medium containing 0.5 M NaCl. Interestingly, the coexpression of ApNhaP with catalase resulted in enhanced salt tolerance of cells grown in sea water. These results demonstrate a key role of sodium ion exclusion by the Na ؉ ͞H ؉ antiporter for the salt tolerance of photosynhetic organisms.Aphanothece halophytica ͉ genetic engineering

show abstract

Section: Methodsmentioning

confidence: 99%

“…PCC 7942 (13)(14)(15). However, the expression of a Na ϩ ͞H ϩ antiporter from Vibrio alginolytica NhaAv resulted in a Na ϩ -sensitive transformant (16).…”

Section: Aphanothece Halophytica ͉ Genetic Engineeringmentioning

confidence: 99%

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Waditee

Hibino

Nakamura

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

122

View full text Add to dashboard Cite

show abstract

“…This effect has been observed in tobacco after the transfer of genes or cDNAs encoding enzymes that lead to the biosynthesis of mannitol, Gly betaine, Pro, trehalose, or fructan (Tarczynski et al, 1993;Kishor et al, 1995;Nomura et al, 1995;Pilon-Smits et al, 1995;Holmstrom et al, 1996). Because many naturally salt-or drought-tolerant plants accumulate such compounds when stressed, these metabolites are considered to be compatible solutes that act by providing osmotic adjustment and by lowering the osmotic potential, i.e.…”

mentioning

confidence: 99%

Increased Salt and Drought Tolerance by D-Ononitol Production in Transgenic Nicotiana tabacum L

et al. 1997

View full text Add to dashboard Cite

The accumulation of high amounts of specific metabolites in transgenic plants increases tolerance to salt and water stress . This effect has been observed in tobacco after the transfer of genes or cDNAs encoding enzymes that lead to the biosynthesis of mannitol, Gly betaine, Pro, trehalose, or fructan (Tarczynski et al., 1993;Kishor et al., 1995;Nomura et al., 1995;Pilon-Smits et al., 1995;Holmstrom et al., 1996). Because many naturally salt-or drought-tolerant plants accumulate such compounds when stressed, these metabolites are considered to be compatible solutes that act by providing osmotic adjustment and by lowering the osmotic potential, i.e. increasing the capacity to retain water (LeRudelier and Boullard, 1983). Other mechanisms by which these metabolites might enhance resistance to stress are, however, still not well understood. Some of these metabolites could act, for example, as scavengers of hydroxyl radicals-extremely toxic, short-lived active oxygen species that have no known enzymatic systems for breakdown (Smirnoff and Cumbes, 1989;Smirnoff, 1993;Asada, 1994;Shen et al., 1997)--or their protective function might be in maintaining the hydration sphere of proteins under water-stress conditions (Galinski, 1993;Papageorgiou and Murata, 1995).We have previously shown that tobacco, transformed to accumulate mannitol, survives high salinity better when stressed at the beginning of the exponential growth phase (Tarczynski et al., 1993). However, the amount of mannitol accumulated was usually not greater than approximately 6 to 8 pmol g-' fresh weight, possibly because of the fact that the Escherickia coli mtlD gene product catalyzed an equilibrium reaction that could also result in a conversion of mannitol-6-P to Fru-6-P, owing to the equal affinity of MtlD for either mannitol-6-P or Fru-6-P (Teschner et al., 1990). The direction of the reaction is determined by a pH-dependent change in affinity for NAD/NADH. W e decided to generate tobacco plants with a capacity for higher polyol production by exploiting a pathway that is induced in the halophyte ice plant (Mesembryantkemum crystallinum) following salt stress (Vernon and Bohnert, 1992). This pathway shunts carbon from Glu-6-P to myoinositol and then to methylated inositols. Methylated inositols are formed by a specific O-methyltransferase, IMT1, which seems to be absent in tobacco. IMTl methylates myo-inositol to form D( +)-ononitol (1D-1-O-methyl-myoinositol). Our expectation was that D-ononitol, which is dependent on the concentration of myo-inositol, might accumulate and provide stress tolerance, but it also seemed possible that the activity of the methyltransferase would generate myo-inositol deficiency.Tobacco (Nicotiana tabacum L., cv SRl) plants, transformed with the IMTl cDNA from M. crystallinum producing the enzyme D-myo-inositol methyltransferase (Vernon et al., 1993), were phenotypically normal. We compare here the physiology of the transformed line, I5A, with untransformed tobacco cv SR1. When the 15A plants were salt stressed or water...

show abstract

“…After 1 week of treatment, samples were taken for quantification of glycinebetaine accumulated in the leaves. Quantification of glycinebetaine was carried out as previously reported (Nomura et aL, 1995).…”

Section: Metabolism Of Exogenously-added Betaine Aldehydementioning

confidence: 99%

Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes

Yokota²,

et al. 1997

View full text Add to dashboard Cite

SummaryBetaine aldehyde dehydrogenase (BADH) catalyzes the last step in the plant biosynthetic pathway that leads to glycinebetaine. Rice plants (Oryza sativa L.}, albeit considered a typical non-glycinebetaine accumulating species, have been found to express this enzyme at low levels. This observation evokes an interest in phylogenic evolution of the enzyme in the plant kingdom. It is reported here that rice plants possess the ability to take up exogenously added betaine aldehyde through the roots and convert it to glycinebetaine, resulting in an enhanced salttolerance of the plants. A gene encoding a putative BADH from the rice genome was also cloned and sequenced. The gene was found to contain 14 introns, and the overall nucleotide sequence of the coding region is c. 78% identical to that of the barley BADH cDNA. Cloning of a partial BADH cDNA from rice was accomplished by reverse transcription-polymerase chain reaction (RT-PCR). The nucleotide sequence of the cloned fragment was found to be identical to the corresponding exon regions of the rice genomic BADH gene. The deduced amino acid sequences of rice and barley BADH both contain a C-terminal tripeptide SKL, a signal known to target preproteins to microbodies. This localization was confirmed by an immuno-gold labeling study of transgenic tobacco harboring barley cDNA, which showed BADH protein inside peroxisomes. Northern blot analysis revealed that the level of BADH mRNA is salt-inducible.

show abstract

Synechococcus sp. PCC7942 Transformed with Escherichia coli bet Genes Produces Glycine Betaine from Choline and Acquires Resistance to Salt Stress

Cited by 115 publications

References 21 publications

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Increased Salt and Drought Tolerance by D-Ononitol Production in Transgenic Nicotiana tabacum L

Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes

Contact Info

Product

Resources

About

Synechococcus sp. PCC7942 Transformed with Escherichia coli bet Genes Produces Glycine Betaine from Choline and Acquires Resistance to Salt Stress

Cited by 115 publications

References 21 publications

Overexpression of a Na + /H + antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Overexpression of a Na + /H + antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Increased Salt and Drought Tolerance by D-Ononitol Production in Transgenic Nicotiana tabacum L

Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes

Contact Info

Product

Resources

About

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water

Overexpression of a Na ⁺ /H ⁺ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water