Tissue- and cell-specific activity of a phenylalanine ammonia-lyase promoter in transgenic plants.

Bevan, Michael W.; Shufflebottom, Diane; Edwards, K. J.; Jefferson, Richard A.; Schuch, Wolfgang

doi:10.1002/j.1460-2075.1989.tb03592.x

Cited by 165 publications

(127 citation statements)

References 35 publications

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“…PAL is an important enzyme in phenylpropanoid metabolic pathway [28], and the expression level of PAL is highly related to the synthesis of flavonoids [3,29]. The role in spatio-temporal expression of Pal promoters have previously been reported [8,11,30]. Our results indicate that PFtPal could drive high level of expression of GUS in chlorenchyma and tissue of root hair zone and root cap in transgenic tobacco.…”

Section: Discussionsupporting

confidence: 62%

Cloning and characterization of a cold inducible Pal promoter from Fagopyrum tataricum

Zhang

Jiang

et al. 2013

Open Life Sciences

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Phenylalanine ammonia-lyase (PAL) catalyzes the first reaction in biosynthesis pathway of flavonoids and plays an important role in plant stress resistance. In this study, the 5’ flanking region of phenylalanine ammonia-lyase gene was isolated from Fagopyrum tataricum by thermal asymmetric interlaced PCR method, named PFtPal (GenBank: KF463139). To investigate the functional properties of PFtPal, we constructed a series of plant expression vectors that contained different promoter fragments resulting from nest deletions and had successfully transformed them into tobacco leaves by Agrobacterium tumefaciens. Histochemical assay of GUS suggested that PFtPal could drive GUS gene expression in leaves and roots, while GUS activity was not detected in the stem. In addition, the region of −274 bp to −1 bp was enough to drive normal expression of GUS gene. Low temperature treatment of transgenic tobacco plants demonstrated that PFtPal conferred cold-induced expression. Taken together, our study will help to better understand the Pal promoter, and provides a candidate promoter for molecular breeding in Fagopyrum plants.

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Section: Discussionsupporting

confidence: 62%

Cloning and characterization of a cold inducible Pal promoter from Fagopyrum tataricum

Zhang

Jiang

et al. 2013

Open Life Sciences

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“…The pine pal sequence is slightly more similar to bean pal-2 than to bean pal-3 at both nucleotide and amino acid levels, an interesting observation in light of the reported expression of the pal-2 gene in differentiating xylem of transgenic tobacco plants (1) and lack of expression of the pal-3 gene in stems of bean (15). The evolutionary relationship of pine pal genes with those of angiosperms is currently under investigation.…”

Section: Gtn-gcn-gcn-gcn-gar-ath-acn-car-qcn-aay-gar-otn-car-gtn-aar-mentioning

confidence: 86%

Phenylalanine Ammonia-Lyase from Loblolly Pine

Whetten¹,

Sederoff²

1992

Plant Physiol.

186

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Phenylalanine ammonia-lyase (EC 4.3.1.5) has been purified from differentiating secondary xylem of loblolly pine (Pinus taeda L.). Native molecular weight of the enzyme was estimated to be 280,000, with a subunit molecular weight of 74,000; isoelectric point, 5.8; and Michaelis constant for i-phenylalanine, 27 micromolar. No evidence was obtained for the existence of isoforms of the enzyme, nor for negative cooperativity of substrate binding. Polyclonal antibodies were raised against the phenylalanine ammonia-lyase subunit and used to identify a pal clone in an expression library of xylem complementary DNA (cDNA). Polymerase chain reaction, using oligonucleotide primers made from N-terminal amino acid sequence and from the 5' end of the clone isolated from the expression library, was also used to isolate cDNA clones. These methods yielded cDNA clones covering the protein coding region of the pal messenger RNA. Comparisons of nucleotide sequence of pal cDNAs from pine, bean, sweet potato, and rice showed 60 to 62% identity between the pine clone and the angiosperm clones.The development of secondary xylem in woody perennials is an interesting biological process that has received little research attention at the molecular level. Inquiry into the processes of wood differentiation has been limited to physiological and ultrastructural studies, which have laid a foundation upon which to build a more detailed understanding of intracellular events. We are beginning to apply tools of molecular biology to problems of xylem differentiation and development that are difficult to address at the level of physiology and ultrastructure.We have chosen to focus on lignification as an important aspect of wood formation. Lignin is a complex polymer of three phenylpropanoid subunits deposited in the cell walls of vascular elements after cell growth has ceased. Sucrose supplied by the phloem is transformed into phenylalanine via the shikimic acid pathway, and lignin monomers are produced from phenylalanine by a branch of phenylpropanoid metabolism. The pathway of lignin precursor biosynthesis is well established (see ref. 7 for review). The first step of the phenylpropanoid pathway is deamination of phenylalanine by ' Supported by the North Carolina State University Forest Biotechnology Industrial Associates Group. PAL2 (EC 4.3.1.5) to yield trans-cinnamic acid. Hydroxylation of cinnamic acid produces p-coumaric acid; additional hydroxylation and methylation of p-coumarate produce first ferulic acid, then sinapic acid. These three acids are coupled to CoA and reduced to the corresponding alcohols. The end products of this pathway are p-coumaryl, coniferyl, and sinapyl alcohols. The relative proportions of the three precursors in lignin varies from species to species and even between cell types within a single individual (14). In general, lignin in angiosperms contains more p-coumaryl and sinapyl alcohol residues than does gymnosperm lignin; coniferyl alcohol is the primary lignin monomer in most gymnosperms.The regulation of ...

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“…The 1.8-kb PALI promoter confers on the uidA reporter gene a specific expression pattern directly associated with the accumulation of anthocyanins. In nonstressed stems, PALI promoter activity is restricted to the protoxylem cells, likely related to lignin deposition (Bevan et al, 1989;Liang et al, 1989). However, in response to low temperature, the promoter is additionally active in cortical cells.…”

Section: Discussionmentioning

confidence: 99%

Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in a Light-Dependent Manner

et al. 1995

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Anthocyanins, which accumulate in leaves and stems in response to low temperature and changes in light intensity, are synthesized through the phenylpropanoid pathway that is controlled by key enzymes that include phenylalanine ammonia-lyase (PAL) and chalcone synthase (CHS). In this work we demonstrate that PAL and CHS mRNAs accumulate in leaves of Arabidopsis thaliana (1.) Heynh. upon exposure to low temperature in a light-dependent manner. The regulation of the PALl gene expression by low temperature and light was examined by analyzing the expression of the P-glucuronidase (uidA) reporter gene in transgenic Arabidopsis plants containing the uidA gene of Escherichia coli under the control of the PALl promoter. The results indicate that the accumulation of PAL 7 mRNA is transcriptionally regulated. Histochemical staining for P-glucuronidase activity showed that the PAL7 promoter i s preferentially activated in photosynthetically active cells, paralleling anthocyanin accumulation. Moreover, we show that light may also be implicated in the regulation of the CHS gene in response to bacterial infiltration. Finally, using two fransparent testa Arabidopsis mutants that are unable to accumulate anthocyanins, we demonstrate that these pigments are not required for successful development of freezing tolerance in this species.

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Tissue- and cell-specific activity of a phenylalanine ammonia-lyase promoter in transgenic plants.

Cited by 165 publications

References 35 publications

Cloning and characterization of a cold inducible Pal promoter from Fagopyrum tataricum

Cloning and characterization of a cold inducible Pal promoter from Fagopyrum tataricum

Phenylalanine Ammonia-Lyase from Loblolly Pine

Low Temperature Induces the Accumulation of Phenylalanine Ammonia-Lyase and Chalcone Synthase mRNAs of Arabidopsis thaliana in a Light-Dependent Manner

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