In situ detection of laccase activity and immunolocalisation of a compression-wood-specific laccase (CoLac1) in differentiating xylem of Chamaecyparis obtusa
Autor: | Saori Sato, Hideto Hiraide, Hiroyuki Yamamoto, Masato Yoshida |
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Rok vydání: | 2016 |
Předmět: |
0106 biological sciences
0301 basic medicine Laccase Oxidase test Xylem Plant Science Biology 01 natural sciences Cell wall 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Biochemistry Tracheid Lignin Monolignol Agronomy and Crop Science Secondary cell wall 010606 plant biology & botany |
Zdroj: | Functional plant biology : FPB. 43(6) |
ISSN: | 1445-4416 |
Popis: | The secondary cell wall of compression wood tracheids has a highly lignified region (S2 L) in its outermost portion. To better understand the mechanism of S2 L formation, we focussed on the activity of laccase (a monolignol oxidase) and performed in situ studies of this enzyme in differentiating compression wood. Staining of differentiating compression wood demonstrated that laccase activity began in all cell wall layers before the onset of lignification. We detected no activity of peroxidase (another monolignol oxidase) in any cell wall layer. Thus, laccase likely plays the major role in monolignol oxidisation during compression wood differentiation. Laccase activity was higher in the S2 L region than in other secondary wall regions, suggesting that this enzyme was responsible for the high lignin concentration in this region of the cell wall. Immunolabelling demonstrated the expression of a compression-wood-specific laccase (CoLac1) immediately following the onset of secondary wall thickening, this enzyme was localised to the S2 L region, whereas much less abundant in the S1 layer or inner S2 layer. Thus, the CoLac1 protein is most likely localised to the outer part of S2 and responsible for the high lignin concentration in the S2 L region. |
Databáze: | OpenAIRE |
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