Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification.

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Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification. / Ostergaard, L; Teilum, K; Mirza, O; Mattsson, O; Petersen, M; Welinder, K G; Mundy, J; Gajhede, M; Henriksen, A.

In: Plant Molecular Biology, Vol. 44, No. 2, 2000, p. 231-43.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Ostergaard, L, Teilum, K, Mirza, O, Mattsson, O, Petersen, M, Welinder, KG, Mundy, J, Gajhede, M & Henriksen, A 2000, 'Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification.', Plant Molecular Biology, vol. 44, no. 2, pp. 231-43.

APA

Ostergaard, L., Teilum, K., Mirza, O., Mattsson, O., Petersen, M., Welinder, K. G., ... Henriksen, A. (2000). Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification. Plant Molecular Biology, 44(2), 231-43.

Vancouver

Ostergaard L, Teilum K, Mirza O, Mattsson O, Petersen M, Welinder KG et al. Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification. Plant Molecular Biology. 2000;44(2):231-43.

Author

Ostergaard, L ; Teilum, K ; Mirza, O ; Mattsson, O ; Petersen, M ; Welinder, K G ; Mundy, J ; Gajhede, M ; Henriksen, A. / Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification. In: Plant Molecular Biology. 2000 ; Vol. 44, No. 2. pp. 231-43.

Bibtex

@article{0b2f9ea093a511dd86a6000ea68e967b,
title = "Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification.",
abstract = "Lignins are phenolic biopolymers synthesized by terrestrial, vascular plants for mechanical support and in response to pathogen attack. Peroxidases have been proposed to catalyse the dehydrogenative polymerization of monolignols into lignins, although no specific isoenzyme has been shown to be involved in lignin biosynthesis. Recently we isolated an extracellular anionic peroxidase, ATP A2, from rapidly lignifying Arabidopsis cell suspension culture and cloned its cDNA. Here we show that the Atp A2 promoter directs GUS reporter gene expression in lignified tissues of transgenic plants. Moreover, an Arabidopsis mutant with increased lignin levels compared to wild type shows increased levels of ATP A2 mRNA and of a mRNA encoding an enzyme upstream in the lignin biosynthetic pathway. The substrate specificity of ATP A2 was analysed by X-ray crystallography and docking of lignin precursors. The structure of ATP A2 was solved to 1.45 A resolution at 100 K. Docking of p-coumaryl, coniferyl and sinapyl alcohol in the substrate binding site of ATP A2 were analysed on the basis of the crystal structure of a horseradish peroxidase C-CN-ferulic acid complex. The analysis indicates that the precursors p-coumaryl and coniferyl alcohols are preferred by ATP A2, while the oxidation of sinapyl alcohol will be sterically hindered in ATP A2 as well as in all other plant peroxidases due to an overlap with the conserved Pro-139. We suggest ATP A2 is involved in a complex regulation of the covalent cross-linking in the plant cell wall.",
author = "L Ostergaard and K Teilum and O Mirza and O Mattsson and M Petersen and Welinder, {K G} and J Mundy and M Gajhede and A. Henriksen",
note = "Keywords: Arabidopsis; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Glucuronidase; Lignin; Models, Molecular; Molecular Sequence Data; Mutation; Peroxidases; Plants, Genetically Modified; Promoter Regions (Genetics); Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Analysis, DNA",
year = "2000",
language = "English",
volume = "44",
pages = "231--43",
journal = "Plant Molecular Biology",
issn = "0167-4412",
publisher = "Springer",
number = "2",

}

RIS

TY - JOUR

T1 - Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification.

AU - Ostergaard, L

AU - Teilum, K

AU - Mirza, O

AU - Mattsson, O

AU - Petersen, M

AU - Welinder, K G

AU - Mundy, J

AU - Gajhede, M

AU - Henriksen, A.

N1 - Keywords: Arabidopsis; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Glucuronidase; Lignin; Models, Molecular; Molecular Sequence Data; Mutation; Peroxidases; Plants, Genetically Modified; Promoter Regions (Genetics); Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Analysis, DNA

PY - 2000

Y1 - 2000

N2 - Lignins are phenolic biopolymers synthesized by terrestrial, vascular plants for mechanical support and in response to pathogen attack. Peroxidases have been proposed to catalyse the dehydrogenative polymerization of monolignols into lignins, although no specific isoenzyme has been shown to be involved in lignin biosynthesis. Recently we isolated an extracellular anionic peroxidase, ATP A2, from rapidly lignifying Arabidopsis cell suspension culture and cloned its cDNA. Here we show that the Atp A2 promoter directs GUS reporter gene expression in lignified tissues of transgenic plants. Moreover, an Arabidopsis mutant with increased lignin levels compared to wild type shows increased levels of ATP A2 mRNA and of a mRNA encoding an enzyme upstream in the lignin biosynthetic pathway. The substrate specificity of ATP A2 was analysed by X-ray crystallography and docking of lignin precursors. The structure of ATP A2 was solved to 1.45 A resolution at 100 K. Docking of p-coumaryl, coniferyl and sinapyl alcohol in the substrate binding site of ATP A2 were analysed on the basis of the crystal structure of a horseradish peroxidase C-CN-ferulic acid complex. The analysis indicates that the precursors p-coumaryl and coniferyl alcohols are preferred by ATP A2, while the oxidation of sinapyl alcohol will be sterically hindered in ATP A2 as well as in all other plant peroxidases due to an overlap with the conserved Pro-139. We suggest ATP A2 is involved in a complex regulation of the covalent cross-linking in the plant cell wall.

AB - Lignins are phenolic biopolymers synthesized by terrestrial, vascular plants for mechanical support and in response to pathogen attack. Peroxidases have been proposed to catalyse the dehydrogenative polymerization of monolignols into lignins, although no specific isoenzyme has been shown to be involved in lignin biosynthesis. Recently we isolated an extracellular anionic peroxidase, ATP A2, from rapidly lignifying Arabidopsis cell suspension culture and cloned its cDNA. Here we show that the Atp A2 promoter directs GUS reporter gene expression in lignified tissues of transgenic plants. Moreover, an Arabidopsis mutant with increased lignin levels compared to wild type shows increased levels of ATP A2 mRNA and of a mRNA encoding an enzyme upstream in the lignin biosynthetic pathway. The substrate specificity of ATP A2 was analysed by X-ray crystallography and docking of lignin precursors. The structure of ATP A2 was solved to 1.45 A resolution at 100 K. Docking of p-coumaryl, coniferyl and sinapyl alcohol in the substrate binding site of ATP A2 were analysed on the basis of the crystal structure of a horseradish peroxidase C-CN-ferulic acid complex. The analysis indicates that the precursors p-coumaryl and coniferyl alcohols are preferred by ATP A2, while the oxidation of sinapyl alcohol will be sterically hindered in ATP A2 as well as in all other plant peroxidases due to an overlap with the conserved Pro-139. We suggest ATP A2 is involved in a complex regulation of the covalent cross-linking in the plant cell wall.

M3 - Journal article

VL - 44

SP - 231

EP - 243

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 2

ER -

ID: 6446876