Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.
Identifieur interne : 002645 ( Main/Corpus ); précédent : 002644; suivant : 002646Putative cationic cell-wall-bound peroxidase homologues in Arabidopsis, AtPrx2, AtPrx25, and AtPrx71, are involved in lignification.
Auteurs : Jun Shigeto ; Yuko Kiyonaga ; Koki Fujita ; Ryuichiro Kondo ; Yuji TsutsumiSource :
- Journal of agricultural and food chemistry [ 1520-5118 ] ; 2013.
English descriptors
- KwdEn :
- Arabidopsis (enzymology), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Cations (MeSH), Cell Wall (enzymology), Isoenzymes (metabolism), Lignin (biosynthesis), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Tyrosine (chemistry).
- MESH :
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Arabidopsis Proteins, Peroxidases, Tyrosine.
- enzymology : Arabidopsis, Cell Wall.
- chemical , genetics : Arabidopsis Proteins, Peroxidases.
- chemical , metabolism : Arabidopsis Proteins, Isoenzymes, Peroxidases.
- chemical : Cations, Oxidation-Reduction.
Abstract
The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls.
DOI: 10.1021/jf400426g
PubMed: 23551275
Links to Exploration step
pubmed:23551275Le document en format XML
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<author><name sortKey="Fujita, Koki" sort="Fujita, Koki" uniqKey="Fujita K" first="Koki" last="Fujita">Koki Fujita</name>
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<author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name>
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<author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name>
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<front><div type="abstract" xml:lang="en">The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls. </div>
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<Abstract><AbstractText>The final step of lignin biosynthesis, which is catalyzed by a plant peroxidase, is the oxidative coupling of the monolignols to growing lignin polymers. Cationic cell-wall-bound peroxidase (CWPO-C) from poplar callus is a unique enzyme that has oxidative activity for both monolignols and synthetic lignin polymers. This study shows that putative CWPO-C homologues in Arabidopsis , AtPrx2, AtPrx25, and AtPrx71, are involved in lignin biosynthesis. Analysis of stem tissue using the acetyl bromide method and derivatization followed by the reductive cleavage method revealed a significant decrease in the total lignin content of ATPRX2 and ATPRX25 deficient mutants and altered lignin structures in ATPRX2, ATPRX25, and ATPRX71 deficient mutants. Among Arabidopsis peroxidases, AtPrx2 and AtPrx25 conserve a tyrosine residue on the protein surface, and this tyrosine may act as a substrate oxidation site as in the case of CWPO-C. AtPrx71 has the highest amino acid identity with CWPO-C. The results suggest a role for CWPO-C and CWPO-C-like peroxidases in the lignification of vascular plant cell walls. </AbstractText>
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