Evidence for isoenzymes of 4-hydroxycinnamic acid: CoA ligase in maize mesocotyls and their response to infection by Helminthosporium maydis race O

Vincent, J. R.; Nicholson, Ralph L.

doi:10.1016/0885-5765(87)90087-7

Cited by 14 publications

(9 citation statements)

References 35 publications

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“…Lignin in pine shows significant microheterogeneity (Terashima and Fukushima, 1988 brock, 1975;Ranjeva et al, 1976;Wallis and Rhodes, 1977;Vincent and Nicholson, 1987). Compression wood is formed in gymnosperms in response to mechanical stress and is characterized by higher wood density, increased lignin content, and an increased proportion of p-coumaryl alcohol-derived components in the compression wood lignin (Timell, 1986).…”

Section: -Coumaratementioning

confidence: 99%

“…They suggested that expression of the different 4CL isozymes could regulate the relative abundance of the three monolignols (coumaryl, coniferyl, and sinapyl alcohols) polymerized into different types of lignin. Isozymes of 4CL were also reported in soybean, petunia, pea, and maize (Knobloch and Hahlbrock, 1975;Ranjeva et al, 1976;Wallis and Rhodes, 1977;Vincent and Nicholson, 1987).…”

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“…4CL has been purified or partially purified from soybean (Knobloch and Hahlbrock, 19751, petunia (Ranjeva et al, 19761, Forsythia (Gross and Zenk, 1974), parsley (Knobloch and Hahlbrock, 1977), poplar (Grand et al, 1983), spruce (Lüderitz et al, 1982), pea (Wallis and Rhodes, 1977), and maize (Vincent and Nicholsori, 1987). DNA sequences encoding 4CL were obtained from parsley (Lozoya et al, 1988), potato (BeckerAndré et al, 1991), rice (Zhao et al, 1990), and soybean (Uhlmann and Ebel, 1993).Lignin in pine shows significant microheterogeneity (Terashima and Fukushima, 1988 brock, 1975;Ranjeva et al, 1976;Wallis and Rhodes, 1977;Vincent and Nicholson, 1987). Compression wood is formed in gymnosperms in response to mechanical stress and is characterized by higher wood density, increased lignin content, and an increased proportion of p-coumaryl alcohol-derived components in the compression wood lignin (Timell, 1986).…”

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4-Coumarate:Coenzyme A Ligase from Loblolly Pine Xylem (Isolation, Characterization, and Complementary DNA Cloning)

et al. 1995

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4-Coumarate:CoA ligase (4CL, EC 6.2.1.12) was purified from differentiating xylem of loblolly pine (Pinus taeda L.). l h e pine enzyme had an apparent molecular mass of 64 kD and was similar in size and kinetic properties to 4CL isolated from Norway spruce. l h e pine enzyme used 4-coumaric acid, caffeic acid, ferulic acid, and cinnamic acid as substrates but had no detectable activity using sinapic acid. 4CL was inhibited by naringenin and coniferin, products of phenylpropanoid metabolism. Although the lignin composition in compression wood is higher in p-hydroxyphenyl units than lignin from normal wood, there was no evidence for a different form of 4CL enzyme in differentiating xylem that was forming compression wood. cDNA clones for 4CL were obtained from a xylem expression library. l h e cDNA sequences matched pine xylem 4CL protein sequences and showed 60 to 66% DNA sequence identity with 4CL sequences from herbaceous angiosperms. lhere were two classes of cDNA obtained from pine xylem, and the genetic analysis showed that they were products of a single gene.The enzyme 4CL (EC 6.2.1.12) catalyzes the formation of COA thioesters of cinnamic acids (Lozoya et al., 1988). Aromatic secondary plant metabolites such as benzoic acid, condensed tannins, lignin precursors, flavonoids, and lignans are a11 derived from the general phenylpropanoid pathway through COA thioesters (Fig. 1). 4CL has been purified or partially purified from soybean (Knobloch and Hahlbrock, 19751, petunia (Ranjeva et al., 19761, Forsythia (Gross and Zenk, 1974), parsley (Knobloch and Hahlbrock, 1977), poplar (Grand et al., 1983), spruce (Lüderitz et al., 1982), pea (Wallis and Rhodes, 1977), and maize (Vincent and Nicholsori, 1987). DNA sequences encoding 4CL were obtained from parsley (Lozoya et al., 1988), potato (BeckerAndré et al., 1991), rice (Zhao et al., 1990), and soybean (Uhlmann and Ebel, 1993).Lignin in pine shows significant microheterogeneity (Terashima and Fukushima, 1988 brock, 1975;Ranjeva et al., 1976;Wallis and Rhodes, 1977;Vincent and Nicholson, 1987). Compression wood is formed in gymnosperms in response to mechanical stress and is characterized by higher wood density, increased lignin content, and an increased proportion of p-coumaryl alcohol-derived components in the compression wood lignin (Timell, 1986). Differences in lignin composition in normal and compression wood of pine could be due to the presence of different isoforms of 4CL in xylem.The objective of this study of 4CL in pine was to determine the number and identity of 4CL isozymes involved in lignin biosynthesis in differentiating xylem. Although we have searched carefully for multiple forms of 4CL by protein purification and cDNA cloning, the weight of our evidence argues for a single 4CL isozyme expressed in loblolly pine (Pinus taeda L.) xylem. 4CL activity was fractionated using five different chromatographic techniques that a11 resolved a single peak of 4CL activity. We demonstrated that the purified 4CL protein had the expected substrate specificit...

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Section: -Coumaratementioning

confidence: 99%

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4-Coumarate:Coenzyme A Ligase from Loblolly Pine Xylem (Isolation, Characterization, and Complementary DNA Cloning)

et al. 1995

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“…For example, 4-coumaroy1:CoA could be directed into flavonoid biosynthesis and different amounts of feruloyl and sinapoy1:CoA directed into the biosynthesis of lignin via distinct 4CL isoforms. In support of this, physically distinct 4CL isoforms have been reported from soybean, petunia, poplar, maize, and parsley (Knobloch and Hahlbrock, 1975;Ranjeva et al, 1976;Grand et al, 1983;Vincent and Nicholson, 1987;Lozoya et al, 1988). Furthermore, in soybean, petunia, and poplar, partially purified 4CL isoforms exhibit different substrate specificities toward substituted cinnamic acids (Knobloch and Hahlbrock, 1975;Ranjeva et al, 1976;Grand et al, 1983).…”

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Two Divergent Members of a Tobacco 4-Coumarate:Coenzyme A Ligase (4CL) Gene Family (cDNA Structure, Gene Inheritance and Expression, and Properties of Recombinant Proteins)

1996

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Severa1 cDNA clones encoding 4-coumarate:coenzyme A ligase (4CL) were isolated from a tobacco (Nicotiana fabacum) cDNA library and grouped into two classes. Sequencing of one cDNA from each class showed that the clones were similar to other 4CL genes and about 80% identical with each other. Cenomic Southern blots using DNA from Nicofiana sylvesfris, Nicofiana fomentosiformis, and N. tabacum demonstrated the presence of both classes of 4CL sequences (4CL7 and 4CL2) in the progenitor species and in tobacco. Northern blots indicated that 4CL mRNA transcripts are highest in old stems and higher in the unpigmented corolla tubes than i n the pigmented limbs of tobacco flowers. The 4CL genes are developmentally regulated and are wound and methyl jasmonate inducible. The relative abilities of recombinant 4CL1 and 4CL2 proteins to utilize 4-coumarate, ferulate, and caffeate as substrates were similar and comparable with that of 4CL in tobacco stem extracts. Surprisingly, both recombinant 4CL proteins utilized cinnamate as a substrate, an activity not observed in stem extracts. This activity was inhibited by a heat-labile, high-molecular-weight factor found in tobacco stem extracts, suggesting that the substrate specificity of 4CL is, in part, determined by the activity of proteinaceous cellular components.The flow of carbon from primary metabolism into the biosynthesis of an array of phenylpropanoid secondary products involves a minimum of three enzymatic steps, catalyzed by the actions of PAL, cinnamate 4-hydroxylase, and 4CL, which collectively form the general phenylpropanoid pathway. The phenylpropanoid products formed by the action of specific downstream branch pathways include coumarins, flavonoids, lignin, suberin, tannins, and other phenolic compounds, which serve diverse functions as phytoalexins, UV protectants, floral and fruit pigments, structural components of cell walls, and signaling molecules (Hahlbrock and Scheel, 1989).As the last enzyme in the general phenylpropanoid pathway, 4CL converts 4-coumaric acid and other hydroxy-or methoxy-derivatives of cinnamic acid, such as caffeic acid,

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“…1, 3) in conifers, is considered to be a key stressresponse enzyme and has been extensively studied in many plant species. 4CL enzymes have been purified or partially purified from soybean and parsley Hahlbrock, 1975, 1977), Forsythia (Gross and Zenk, 1974), petunia (Ranjeva et al, 1976), pea (Wallis and Rhodes, 1977), spruce (Lüderitz et al, 1982), poplar (Grand et al, 1983), maize (Vincent and Nicholson, 1987), and loblolly pine (Pinus taeda L., Voo et al, 1995). The cDNA sequences have been reported for parsley (Lozoya et al, 1988), potato (BeckerAndré et al, 1991), soybean (Uhlmann and Ebel, 1993), loblolly pine (Voo et al, 1995), Arabidopsis (Lee et al, 1995), aspen (Kawaoka and Chiang, 1996), and tobacco (Lee and Douglas, 1996).…”

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Molecular Cloning of 4-Coumarate:Coenzyme A Ligase in Loblolly Pine and the Roles of This Enzyme in the Biosynthesis of Lignin in Compression Wood

1997

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Two genomic sequences encoding 4-coumarate:coenzyme A ligase (4CL; EC 6.2.1.1 2) in loblolly pine (Pinus faeda 1.) were cloned. Both sequences contained three introns and four exons with identical coding sequences predicting 537 amino acids. Two of the three introns in these two clones were different both in sequence and in length. Sequences of both 4CL clones were found in all nine megagametophyte DNAs tested, providing genetic evidence that these two 4CL genomic sequences are nonallelic genes. Our analyses suggest that there are at least two distinct, intron-containing 4CL genes, at least one of which is transcribed into 4CL mRNA in developing xylem tissue of loblolly pine. The levels of 4CL gene transcription in xylem were influenced by compressional stress, resulting in an elevated 4CL enzyme activity with 4-coumaric acid. 4CL enzyme activity with ferulic acid remained unchanged, whereas with caffeic acid it was significantly inhibited. Exogenously applied trans-cinnamic acid in the protein extracts from normal wood xylem caused inhibition of 4CL activity toward caffeic acid similar to that under compressional stress. The implications of this cinnamic acid-modulated effect on 4CL enzyme activities toward different substrates in regulating monolignol synthesis in xylem under compressional stress are discussed.

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Evidence for isoenzymes of 4-hydroxycinnamic acid: CoA ligase in maize mesocotyls and their response to infection by Helminthosporium maydis race O

Cited by 14 publications

References 35 publications

4-Coumarate:Coenzyme A Ligase from Loblolly Pine Xylem (Isolation, Characterization, and Complementary DNA Cloning)

4-Coumarate:Coenzyme A Ligase from Loblolly Pine Xylem (Isolation, Characterization, and Complementary DNA Cloning)

Two Divergent Members of a Tobacco 4-Coumarate:Coenzyme A Ligase (4CL) Gene Family (cDNA Structure, Gene Inheritance and Expression, and Properties of Recombinant Proteins)

Molecular Cloning of 4-Coumarate:Coenzyme A Ligase in Loblolly Pine and the Roles of This Enzyme in the Biosynthesis of Lignin in Compression Wood

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