Transcription of two members of a gene family encoding phenylalanine ammonia‐lyase leads to remarkably different cell specificities and induction patterns

Shufflebottom, Diane; Edwards, Keith J.; Schuch, Wolfgang; Bevan, Michael W.

doi:10.1111/j.1365-313x.1993.00835.x

Cited by 78 publications

(27 citation statements)

References 51 publications

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“…In a recent study, Shufflebottom et al (1993) compared the transcriptional activities of bean PAL2 and PAL3 genes by fusing their promoters to the GUS gene and transforming Arabidopsis, tobacco and potato with these constructs. The PAL2 and PAL3 promoters direct both different and overlapping patterns of GUS expression.…”

Section: {B) Phenylalaninementioning

confidence: 99%

Biochemistry and molecular biology of lignification

1995

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SUMMARY Lignins, which result from the dehydrogenative polymerization of cinnamyl alcohols, are complex heteropolymers deposited in the walls of specific cells of higher plants. Lignins have probably been associated to land colonization by plants but several aspects concerning their biosynthesis, structure and function are still only partially understood. This review focuses on the modern physicochemical methods of structural analysis of lignins, and on the new approaches of molecular biology and genetic engineering applied to lignification. The principles, advantages and limitations of three important analytical tools for studying lignin structure are presented. They include carbon 13 nuclear magnetic resonance, analytical pyrolysis and thioacidolysis. The use of these methods is illustrated by several examples concerning the characterization of grass lignins,‘lignin‐like’materials in protection barriers of plants and lignins produced by cell suspension cultures. Our present limited knowledge of the spatio temporal deposition of lignins during cell wall differentiation including the nature of the wall components associated to lignin deposition and of the cross‐links between the different wall polymers is briefly reviewed. Emphasis is placed on the phenylpropanoid pathway enzymes and their corresponding genes which are described in relation to their potential roles in the quantitative and qualitative control of lignification. Recent findings concerning the promoter sequence elements responsible for the vascular expression of some of these genes are presented. A section is devoted to the enzymes specifically involved in the synthesis of monolignols: cinnamoyl CoA reductase and cinnamyl alcohol dehydrogenase. The recent characterization of the corresponding cDNAs/genes offers new possibilities for a better understanding of the regulation of lignification. Finally, at the level of the synthesis, the potential involvement of peroxidases and laccases in the polymerization of monolignols is critically discussed. In addition to previously characterized naturally occurring lignin mutants, induced lignin mutants have been obtained during the last years through genetic engineering. Some examples include plants transformed by O‐methyltransferase and cinnamyl alcohol dehydrogenase antisense constructs which exhibit modified lignins. Such strategies offer promising perspectives in gaining a better understanding of lignin metabolism and functions and represent a realistic way to improve plant biomass.

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Section: {B) Phenylalaninementioning

confidence: 99%

Biochemistry and molecular biology of lignification

1995

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“…Trans-cinnamic acid, in turn, is the common precursor for the lignin and flavonoids biosynthetic pathways, which are highly complex and branched pathways [7]. Increased activity of PAL has been correlated with increased production of phenylpropanoid products [8], and levels of PAL activity vary with developmental stage, cell and tissue differentiation, and exposure to different stress stimuli [9-11]. PAL has been reported to be stimulated by infection, mechanical wounding, UV irradiation, drought stress and drastic temperature changes [12-14].…”

Section: Introductionmentioning

confidence: 99%

The phenylalanine ammonia lyase (PAL) gene family shows a gymnosperm-specific lineage

et al. 2012

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Background Phenylalanine ammonia lyase (PAL) is a key enzyme of the phenylpropanoid pathway that catalyzes the deamination of phenylalanine to trans-cinnamic acid, a precursor for the lignin and flavonoid biosynthetic pathways. To date, PAL genes have been less extensively studied in gymnosperms than in angiosperms. Our interest in PAL genes stems from their potential role in the defense responses of Pinus taeda , especially with respect to lignification and production of low molecular weight phenolic compounds under various biotic and abiotic stimuli. In contrast to all angiosperms for which reference genome sequences are available, P. taeda has previously been characterized as having only a single PAL gene. Our objective was to re-evaluate this finding, assess the evolutionary history of PAL genes across major angiosperm and gymnosperm lineages, and characterize PAL gene expression patterns in Pinus taeda . Methods We compiled a large set of PAL genes from the largest transcript dataset available for P. taeda and other conifers. The transcript assemblies for P. taeda were validated through sequencing of PCR products amplified using gene-specific primers based on the putative PAL gene assemblies. Verified PAL gene sequences were aligned and a gene tree was estimated. The resulting gene tree was reconciled with a known species tree and the time points for gene duplication events were inferred relative to the divergence of major plant lineages. Results In contrast to angiosperms, gymnosperms have retained a diverse set of PAL genes distributed among three major clades that arose from gene duplication events predating the divergence of these two seed plant lineages. Whereas multiple PAL genes have been identified in sequenced angiosperm genomes, all characterized angiosperm PAL genes form a single clade in the gene PAL tree, suggesting they are derived from a single gene in an ancestral angiosperm genome. The five distinct PAL genes detected and verified in P. taeda were derived from a combination of duplication events predating and postdating the divergence of angiosperms and gymnosperms. Conclusions Gymnosperms have a more phylogenetically diverse set of PAL genes than angiosperms. This inference has contrasting implications for the evolution of PAL gene function in gymnosperms and angiosperms.

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“…Four distinct PAL genes in each haploid genome were demonstrated in parsley (Lois et al, 1989), three to four in french bean (Phaseolus vulgaris L.; Cramer et al, 1989), four to five in Arubidopsis thaliana (Oh1 et al, 1990), five in tomato (Lycopersicon esculentum L.; Lee et al, 1992) and approximately 40-50 in potato (Solanum tuberosum L. ; Joos and Hahlbrock, 1992). In some cases, differential expression of individual PAL genes has been demonstrated (Liang et al, 1989;Lois and Hahlbrock, 1992;Shufflebottom et al, 1993). In all plants studied, PAL was shown to occur as a tetrameric enzyme (Havir and Hanson, 1973), and multiple tetrameric forms with slightly different molecular masses, PI and K,,, values have been isolated from various whole-plant tissues as well as suspension-cultured cells (Bollwell et al, 1985).…”

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confidence: 99%

Structural and Catalytic Properties of the Four Phenylalanine Ammonia‐Lyase Isoenzymes from Parsley (Petroselinum Crispum Nym.)

Appert¹,

Logemann²,

Hahlbrock³

et al. 1994

European Journal of Biochemistry

121

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Near-full-length cDNAs for the four phenylalanine ammonia-lyase (PAL) isoenzymes in parsley (Petruselinum crispum Nym.) were cloned and the complete amino acid sequences deduced. Fusion proteins with glutathione S-transferase were expressed in Escherichia coli, purified and cleaved. All of the resulting phenylalanine ammonia-lyase proteins, as well as the fusion proteins, were catalytically active. The turnover number of one selected isoenzyme, PAL-1, was estimated to be around 22 s-' for each active site. In contrast to a certain degree of differential expression in various parts of parsley plants, the four phenylalanine ammonia-lyase isoenzymes exhibited very similar apparent K,,, values for L-phenylalanine (15-24.5 pM) as well as identical temperature (58°C) and pH (8.5) optima. All of them were competitively inhibited by (E)-cinnamate with similar efficiency (K, values: 9

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Transcription of two members of a gene family encoding phenylalanine ammonia‐lyase leads to remarkably different cell specificities and induction patterns

Cited by 78 publications

References 51 publications

Biochemistry and molecular biology of lignification

Biochemistry and molecular biology of lignification

The phenylalanine ammonia lyase (PAL) gene family shows a gymnosperm-specific lineage

Structural and Catalytic Properties of the Four Phenylalanine Ammonia‐Lyase Isoenzymes from Parsley (Petroselinum Crispum Nym.)

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