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Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase

L. M. Lagrimini
- 01 Jun 1991 - 
- Vol. 96, Iss: 2, pp 577-583
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TLDR
Lignin deposition in wounded pith tissue from control plants closely followed the induction of peroxidase activity, however, wound-induced lignification occurred 24 to 48 hours sooner in plants overexpressing the anionic per oxidase.
Abstract
Tobacco (Nicotiana tabacum) plants transformed with a chimeric tobacco anionic peroxidase gene have previously been shown to synthesize high levels of peroxidase in all tissues throughout the plant. One of several distinguishable phenotypes of transformed plants is the rapid browning of pith tissue upon wounding. Pith tissue from plants expressing high levels of peroxidase browned within 24 hours of wounding, while tissue from control plants did not brown as late as 7 days after wounding. A correlation between peroxidase activity and wound-induced browning was observed, whereas no relationship between polyphenol oxidase activity and browning was found. The purified tobacco anionic peroxidase was subjected to kinetic analysis with substrates which resemble the precursors of lignin or polyphenolic acid. The purified enzyme was found to readily polymerize phenolic acids in the presence of H2O2 via a modified ping-pong mechanism. The percentage of lignin and lignin-related polymers in cell walls was nearly twofold greater in pith tissue isolated from peroxidase-overproducer plants compared to control plants. Lignin deposition in wounded pith tissue from control plants closely followed the induction of peroxidase activity. However, wound-induced lignification occurred 24 to 48 hours sooner in plants overexpressing the anionic peroxidase. This suggests that the availability of peroxidase rather than substrate may delay polyphenol deposition in wounded tissue.

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Citations
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Phytotoxicity of BDE-28, BDE-47 and BDE-99 to maize (Zea mays L.) during germination and early growth

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Patent

SEQUENCES D'ADN CODANT POUR UNE CINNAMOYL CoA REDUCTASE, ET LEURS APPLICATIONS DANS LE DOMAINE DE LA REGULATION DES TENEURS EN LIGNINES DES PLANTES

TL;DR: The authors concerne toute sequence d'ADNodes comprenant a titre de region codante, tout ou partie de la sequence nucleotidique codant for un ARNm antisens susceptible de s'hybrider avec l'ARNm susmentionne.
References
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Journal ArticleDOI

Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: molecular analysis and tissue-specific expression

TL;DR: The purification of the anionic peroxidase isozymes from tobacco and their partial amino acid sequence is reported and the messenger for the tobacco isozyme was found to be abundant in stem tissue while expressed at very low levels in leaf and root tissue.
Journal ArticleDOI

Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue.

TL;DR: The present results support the hypothesis that this anionic peroxidase is involved in the deposition of the aromatic polymeric domain of suberin.
Journal ArticleDOI

Tissue Specificity of Tobacco Peroxidase Isozymes and Their Induction by Wounding and Tobacco Mosaic Virus Infection

TL;DR: To determine which peroxidase isozymes from Nicotiana tabacum are involved in cell wall biosynthesis or other normal cellular functions and which respond to stress, plants were subjected to either wounding or infection with tobacco mosaic virus.
Journal ArticleDOI

Immunocytolocalization of extensin in developing soybean seed coats by immunogold-silver staining and by tissue printing on nitrocellulose paper.

TL;DR: In soybean seed coats the accumulation of the hydroxyproline-rich glycoprotein extensin is regulated in a developmental and tissue- specific manner and is primarily localized in the seed coat, hilum, and vascular elements of the seed.
Journal ArticleDOI

Preparation and microbial decomposition of synthetic [14C]ligins.

TL;DR: A definitive assay for microbiological and biochemical research on the biodegradation of lignin was developed using radioactive synthetic lignins specifically labeled in the side chains, aromatic rings or in the methoxyl groups.
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