A cDNA Encoding Farnesyl Pyrophosphate Synthase in White Lupin

Attucci, Sylvie; Aitken, Susan-Marie; Ibrahim, Ragai K.; Gulick, Patrick J.

doi:10.1104/pp.108.2.835

Cited by 34 publications

(10 citation statements)

References 7 publications

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“…3. Alignment of the deduced amino acid sequences of FDP synthase of Hevea (hevfps), Arabidopsis (arathfps) [ 17], lupin (lupinfps) [7], yeast (yeastfps) [2], rat (ratfps) [6] and man (humfpsl) [40]. Consensus sequences are shaded.…”

Section: 1 T T T G C T T C G C a A T C A C A T T C C C A G G A T T mentioning

confidence: 99%

Cloning and characterization of cDNA encoding farnesyl diphosphate synthase from rubber tree (Hevea brasiliensis)

Adiwilaga

Kush

1996

Plant Mol Biol

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Commercially used natural rubber (cis-1,4-polyisoprene) is a secondary metabolite of the rubber tree (Hevea brasiliensis). Previous studies have shown the involvement of a prenyl transferase in the final steps of natural rubber biosynthesis which includes polymerization of isopentenyl pyrophosphate into rubber. Using synthetic oligonucleotides corresponding to the partial amino acid sequences of this protein as probes to screen a laticifer-specific cDNA library, we have isolated a full-length cDNA which encodes a 47 kDa protein with strong homology to farnesyl diphosphate synthases from many species. The catalytic activity of this protein was confirmed by complementing the deletion yeast mutant. In Hevea, this gene is expressed in latex producing cells and in the epidermal region of the rubber plant suggesting a dual role for the protein in the biosyntheses of rubber and other isoprenoids. Although the expression level of this gene is not significantly affected by hormone treatment (e.g. ethylene), regeneration of latex due to tapping increases its expression level.

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Section: 1 T T T G C T T C G C a A T C A C A T T C C C A G G A T T mentioning

confidence: 99%

Cloning and characterization of cDNA encoding farnesyl diphosphate synthase from rubber tree (Hevea brasiliensis)

Adiwilaga

Kush

1996

Plant Mol Biol

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“…Plant FPS has been purified and characterized from different species (1,15,16) and, recently, cDNA sequences encoding this enzyme have been cloned from Arabidopsis thaliana (17) and Lupinus albus (18,19). Comparison of the amino acid sequences of FPS from a variety of organisms, ranging from bacteria to higher eukaryotes, has shown that all the FPS known so far contain five distinct regions with high similarity at the amino acid level (19,20).…”

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confidence: 99%

Arabidopsis thaliana Contains Two Differentially Expressed Farnesyl-Diphosphate Synthase Genes

Cunillera

Arró

Delourme

et al. 1996

Journal of Biological Chemistry

162

128

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“…9, based on sequence similarity at the amino acid level. As can be seen in cluster 1, all of the PLRs group together, along with a "homolog" from Lupinus albus (14), which may also encode a PLR. The IFRs, together with the "homolog" from Glycine max, 7 also form a cluster (cluster 2), suggesting that IFRHGm1 may in fact be an isoflavone reductase.…”

Section: Resultsmentioning

confidence: 99%

Evolution of Plant Defense Mechanisms

Gang¹,

Kasahara²,

Xia³

et al. 1999

Journal of Biological Chemistry

176

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Pinoresinol-lariciresinol and isoflavone reductase classes are phylogenetically related, as is a third, the so-called "isoflavone reductase homologs." This study establishes the first known catalytic function for the latter, as being able to engender the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Accordingly, all three reductase classes are involved in the biosynthesis of important and related phenylpropanoidderived plant defense compounds. In this investigation, the phenylcoumaran benzylic ether reductase from the gymnosperm, Pinus taeda, was cloned, with the recombinant protein heterologously expressed in Escherichia coli. The purified enzyme reduces the benzylic ether functionalities of both dehydrodiconiferyl alcohol and dihydrodehydrodiconiferyl alcohol, with a higher affinity for the former, as measured by apparent K m and V max values and observed kinetic 3 H-isotope effects. It abstracts the 4R-hydride of the required NADPH cofactor in a manner analogous to that of the pinoresinol-lariciresinol reductases and isoflavone reductases. A similar catalytic function was observed for the corresponding recombinant reductase whose gene was cloned from the angiosperm, Populus trichocarpa. Interestingly, both pinoresinol-lariciresinol reductases and isoflavone reductases catalyze enantiospecific conversions, whereas the phenylcoumaran benzylic ether reductase only shows regiospecific discrimination. A possible evolutionary relationship among the three reductase classes is proposed, based on the supposition that phenylcoumaran benzylic ether reductases represent the progenitors of pinoresinol-lariciresinol and isoflavone reductases.

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A cDNA Encoding Farnesyl Pyrophosphate Synthase in White Lupin

Cited by 34 publications

References 7 publications

Cloning and characterization of cDNA encoding farnesyl diphosphate synthase from rubber tree (Hevea brasiliensis)

Cloning and characterization of cDNA encoding farnesyl diphosphate synthase from rubber tree (Hevea brasiliensis)

Arabidopsis thaliana Contains Two Differentially Expressed Farnesyl-Diphosphate Synthase Genes

Evolution of Plant Defense Mechanisms

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