Expression of Mangrove Allene Oxide Cyclase Enhances Salt Tolerance in Escherichia coli, Yeast, and Tobacco Cells

Yamada, Akiyo; Saitoh, Takeo; Mimura, Tetsuro; Ozeki, Yoshihiro

doi:10.1093/pcp/pcf108

Cited by 84 publications

(61 citation statements)

References 23 publications

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“…1B). A similar situation has been reported for the allene oxide cyclase homologue ("mangrin") from the mangrove, Bruguiera sexangula (44), wherein a stretch of 70 amino acid residues, different in its organization from the allene oxide cyclase from Arabidopsis or Lycopersicum, conferred salt tolerance to E. coli, yeast, and tobacco cells. Furthermore, whether the PINO1 gene is the only MIPS-coding gene in Porteresia or a duplicated paralogue of INO1 having a different organization has yet to be resolved.…”

Section: Discussionsupporting

confidence: 70%

“…We have chosen the enzyme MIPS, which is conserved across evolutionarily diverse taxa (4,12), produces inositol, and is known to function in varied biochemical activities and also during stress in both prokaryotic and eukaryotic organisms (3,(41)(42)(43)(44)(45). Among the 65 INO1 genes known (12), the INO1 from Archaeoglobus fulgidis (11) has been shown to code for a thermotolerant protein, the only stress-tolerant MIPS so far reported.…”

Section: Discussionmentioning

confidence: 99%

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A Novel Salt-tolerant l-myo-Inositol-1-phosphate Synthase from Porteresia coarctata (Roxb.) Tateoka, a Halophytic Wild Rice

Majee

Maitra

Dastidar

et al. 2004

Journal of Biological Chemistry

173

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L-myo-Inositol-1-phosphate synthase (EC 5.5.1.4, MIPS), an evolutionarily conserved enzyme protein, catalyzes the synthesis of inositol, which is implicated in a number of metabolic reactions in the biological kingdom. Here we report on the isolation of the gene (PINO1) for a novel salt-tolerant MIPS from the wild halophytic rice, Porteresia coarctata (Roxb.) Tateoka. Identity of the PINO1 gene was confirmed by functional complementation in a yeast inositol auxotrophic strain. Comparison of the nucleotide and deduced amino acid sequences of PINO1 with that of the homologous gene from Oryza sativa L. (RINO1) revealed distinct differences in a stretch of 37 amino acids, between amino acids 174 and 210. Purified bacterially expressed PINO1 protein demonstrated a salt-tolerant character in vitro compared with the salt-sensitive RINO1 protein as with those purified from the native source or an expressed salt-sensitive mutant PINO1 protein wherein amino acids 174 -210 have been deleted. Analysis of the salt effect on oligomerization and tryptophan fluorescence of the RINO1 and PINO1 proteins revealed that the structure of PINO1 protein is stable toward salt environment. Furthermore, introgression of PINO1 rendered transgenic tobacco plants capable of growth in 200 -300 mM NaCl with retention of ϳ40 -80% of the photosynthetic competence with concomitant increased inositol production compared with unstressed control. MIPS protein isolated from PINO1 transgenics showed salt-tolerant property in vitro confirming functional expression in planta of the PINO1 gene. To our knowledge, this is the first report of a salt-tolerant MIPS from any source.Inositols are six-carbon cyclohexane hexitols found ubiquitously in the biological kingdom, and its metabolism plays a vital role in growth regulation, membrane biogenesis, osmotolerance, and in many other processes. As phosphorylated derivatives, its role as a phosphorus store and as a "second messenger" in signal transduction pathways has long been recognized. myo-Inositol, physiologically the most favored stereoisomer among the eight possible geometric isomers of inositol, also enters into an array of biochemical reactions having diverse functions in cellular metabolism both as free and conjugated and phosphorylated or methylated forms (1-3).The primary enzyme for the synthesis of L-myo-inositol 1-phosphate from glucose 6-phosphate is L-myo-inositol-1-phosphate synthase (EC 5.5.1.4; referred to as MIPS), 1 which synthesizes L-myo-inositol 1-phosphate through an internal oxidoreduction reaction involving NAD ϩ . Free inositol is generated by dephosphorylation of the MIPS product by a specific Mg 2ϩ -dependent inositol-1-phosphate phosphatase (EC 3.1.3.25). This mechanism is followed by all myo-inositolproducing organisms throughout the phylogenetic lines, and MIPS has been identified as an evolutionarily conserved protein (4). The structural gene coding for cytosolic MIPS, termed INO1, was first identified in yeast, Saccharomyces cerevisiae (5, 6) and cloned by Klig and Henry (7)....

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Section: Discussionsupporting

confidence: 70%

Section: Discussionmentioning

confidence: 99%

A Novel Salt-tolerant l-myo-Inositol-1-phosphate Synthase from Porteresia coarctata (Roxb.) Tateoka, a Halophytic Wild Rice

Majee

Maitra

Dastidar

et al. 2004

Journal of Biological Chemistry

173

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“…Data are averages of the percent differences from the control in three wells, with SE. on salt (NaCl) tolerance mechanisms (Yamada et al 2002). Little information has been available concerning the halophilic nature and the cellular mechanisms of the suspension cultures of Avicenniaceae species.…”

Section: Ca 2ϩmentioning

confidence: 99%

Stimulatory effects of sea salts on cell growth in liquid culture of Avicenniaceae mangrove

Hayashi

Kuriyama

Kawana

et al. 2009

Plant Biotechnology

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“…Poir. and converted it in Escherichia coli, yeasts, and tobacco, improving the salt tolerance of the obtained transformant [34] . Yu et al converted the salt-tolerant gene mangrin into Eucalyptus and also acquired a transformant with enhanced salt tolerance [35] .…”

Section: Discussionmentioning

confidence: 99%

Cloning of SjCA gene and its expression analysis on upland cottons

Kong

Zhao

et al. 2016

JBEI

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Acquisition of salt-tolerant genes from exogenous plants to improve cotton salt resistance has always been a hotspot of research on cotton salt resistance. However, the information regarding the method of conversion of living cotton pollens by portable gene gun technology is still little. Complete sequence information of the Carbonic Anhydrase (CA) gene was obtained from NCBI database, and its full ORF length sequence was cloned by RT-PCR technology. After the construction of pBI121-CA::GFP fusion expression vector, we used cotton pollens from upland cotton varieties Y-2067, ZA-23, and GZ-2, which have weaker autofluorescence, to conduct the research on the transient expression of cotton pollens in vivo via particle bombardment (gene gun technology). The results indicated that green fluorescence enhancement of the three kinds of cotton pollens was realized after the CA gene transformation, meaning that the CA gene expression level was increased. Besides, the salt tolerance germination ability of transgenic T1 seeds was also improved. Our research initially established a transient expression system of cotton pollen in vivo via particle bombardment technology, laying the theoretical foundation for further research of cotton genetic transformation and creation of cotton salt-tolerant germplasm.

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Expression of Mangrove Allene Oxide Cyclase Enhances Salt Tolerance in Escherichia coli, Yeast, and Tobacco Cells

Cited by 84 publications

References 23 publications

A Novel Salt-tolerant l-myo-Inositol-1-phosphate Synthase from Porteresia coarctata (Roxb.) Tateoka, a Halophytic Wild Rice

A Novel Salt-tolerant l-myo-Inositol-1-phosphate Synthase from Porteresia coarctata (Roxb.) Tateoka, a Halophytic Wild Rice

Stimulatory effects of sea salts on cell growth in liquid culture of Avicenniaceae mangrove

Cloning of SjCA gene and its expression analysis on upland cottons

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