4.6 Article

PtomtAPX is an autonomous lignification peroxidase during the earliest stage of secondary wall formation in Populus tomentosa Carr

Journal

NATURE PLANTS
Volume 8, Issue 7, Pages 828-839

Publisher

NATURE PORTFOLIO
DOI: 10.1038/s41477-022-01181-3

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Funding

  1. Natural Science Foundation of China [31971618]
  2. National Key Research and Development Program of China [2021YFD2200900]
  3. National Research Foundation of Korea [4120200313623] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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This study reveals the crucial role of mitochondrial ascorbate peroxidase in catalyzing lignin polymerization during the early stages of secondary cell wall formation. It also describes how xylem cells provide autonomous enzymes needed for lignin polymerization by coupling with the programmed cell death process.
At present, a cooperative process hypothesis is used to explain the supply of enzyme (class III peroxidases and/or laccases) and substrates during lignin polymerization. However, it remains elusive how xylem cells meet the needs of early lignin rapid polymerization during secondary cell wall formation. Here we provide evidence that a mitochondrial ascorbate peroxidase (PtomtAPX) is responsible for autonomous lignification during the earliest stage of secondary cell wall formation in Populus tomentosa. PtomtAPX was relocated to cell walls undergoing programmed cell death and catalysed lignin polymerization in vitro. Aberrant phenotypes were caused by altered PtomtAPX expression levels in P. tomentosa. These results reveal that PtomtAPX is crucial for catalysing lignin polymerization during the early stages of secondary cell wall formation and xylem development, and describe how xylem cells provide autonomous enzymes needed for lignin polymerization during rapid formation of the secondary cell wall by coupling with the programmed cell death process. Mitochondrial ascorbate peroxidase (PtomtAPX) is relocated to cell walls undergoing programmed cell death and catalyses lignin polymerization. These results show how xylem cells provide autonomous enzymes needed for lignin polymerization.

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