Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce

Kurt V. Fagerstedt (Corresponding Author), Eija M. Kukkola, Ville V. T. Koistinen, Junko Takahashi, Kaisa Marjamaa

Research output: Contribution to journalArticleScientificpeer-review

68 Citations (Scopus)

Abstract

Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT‐)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.
Original languageEnglish
Pages (from-to)186-194
Number of pages9
JournalJournal of Integrative Plant Biology
Volume52
Issue number2
DOIs
Publication statusPublished - 2010
MoE publication typeA1 Journal article-refereed

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Peroxidases
Lignin
peroxidases
Norway
Polymerization
Cell Wall
Picea abies
Xylem
lignin
Cells
cell walls
polymerization
Genes
Abies
Picea
xylem
Plant Genes
Tissue culture
Tobacco
lignin peroxidase

Cite this

Fagerstedt, Kurt V. ; Kukkola, Eija M. ; Koistinen, Ville V. T. ; Takahashi, Junko ; Marjamaa, Kaisa. / Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce. In: Journal of Integrative Plant Biology. 2010 ; Vol. 52, No. 2. pp. 186-194.
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title = "Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce",
abstract = "Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT‐)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.",
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Cell wall lignin is polymerised by class III secretable plant peroxidases in Norway spruce. / Fagerstedt, Kurt V. (Corresponding Author); Kukkola, Eija M.; Koistinen, Ville V. T.; Takahashi, Junko; Marjamaa, Kaisa.

In: Journal of Integrative Plant Biology, Vol. 52, No. 2, 2010, p. 186-194.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Fagerstedt, Kurt V.

AU - Kukkola, Eija M.

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AU - Takahashi, Junko

AU - Marjamaa, Kaisa

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AB - Class III secretable plant peroxidases occur as a large family of genes in plants with many functions and probable redundancy. In this review we are concentrating on the evidence we have on the catalysis of lignin polymerization by class III plant peroxidases present in the apoplastic space in the xylem of trees. Some evidence exists on the specificity of peroxidase isozymes in lignin polymerization through substrate specificity studies, from antisense mutants in tobacco and poplar and from tissue and cell culture lines of Norway spruce (Picea abies) and Zinnia elegans. In addition, real time (RT‐)PCR results have pointed out that many peroxidases have tissue specific expression patterns in Norway spruce. Through combining information on catalytic properties of the enzymes, on the expression patterns of the corresponding genes, and on the presence of monolignols and hydrogen peroxide in the apoplastic space, we can show that specific peroxidases catalyze lignin polymerization in the apoplastic space of Norway spruce xylem.

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