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A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis






Plant journal: for cell and molecular biology 27(2): 89-99

A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis

We isolated an Arabidopsis lesion initiation 2 (lin2) mutant, which develops lesion formation on leaves and siliques in a developmentally regulated and light-dependent manner. The phenotype of the lin2 plants resulted from a single nuclear recessive mutation, and LIN2 was isolated by a T-DNA tagging approach. LIN2 encodes coproporphyrinogen III oxidase, a key enzyme in the biosynthetic pathway of chlorophyll and heme, a tetrapyrrole pathway, in Arabidopsis. The lin2 plants express cytological and molecular markers associated with the defense responses, usually activated by pathogen infection. These results demonstrate that a porphyrin pathway impairment is responsible for the lesion initiation phenotype, which leads to the activation of defense responses, in Arabidopsis. Lesion formation was not suppressed, and was even enhanced when accumulation of salicylic acid (SA) was prevented in lin2 plants by the expression of an SA-degrading salicylate hydroxylase (nahG) gene. This suggests that the lesion formation triggered in lin2 plants is determined prior to or independently of the accumulation of SA but that the accumulation is required to limit the spread of lesions in lin2 plants.

Accession: 003342549

PMID: 11489187

DOI: 10.1046/j.1365-313x.2001.01058.x

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Related references

Ishikawa, A.; Okamoto, H.; Iwasaki, Y.; Asahi, T., 2001: A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis. We isolated an Arabidopsis lesion initiation 2 (lin2) mutant, which develops lesion formation on leaves and siliques in a developmentally regulated and light-dependent manner. The phenotype of the lin2 plants resulted from a single nuclear recessi...

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Hawk, J.L.; Magnus, I.A.; Parkes, A.; Elder, G.H.; Doyle, M., 1978: Deficiency of hepatic coproporphyrinogen oxidase in hereditary coproporphyria. Journal of the Royal Society of Medicine 71(10): 775-777

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Elder, G.H.; Evans, J.O.; Jackson, J.R.; Jackson, A.H., 1978: Factors determining the sequence of oxidative decarboxylation of the 2- and 4-propionate substituents of coproporphyrinogen III by coproporphyrinogen oxidase in rat liver. Coproporphyrinogen oxidase (EC 1.3.3.3) catalyses the oxidative decarboxylation of the 2- and 4-propionate substituents of coproporphyrinogen III to form protoporphyrinogen IX. A 4-propionate-substituted porphyrinogen, harderoporphyrinogen, which...

Rand, K.; Noll, C.; Schiebel, H.Martin.; Kemken, D.; Dülcks, T.; Kalesse, M.; Heinz, D.W.; Layer, G., 2010: The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX. During heme biosynthesis the oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of the two propionate side chains on rings A and B of coproporphyrinogen III to the corresponding vinyl groups to yield pro...

Lash, T.D.; Kaprak, T.A.; Shen, L.; Jones, M.A., 2002: Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase. Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions...

Lash, T.D.; Kaprak, T.A.; Shen, L.; Jones, M.A., 2002: Metabolism of analogues of coproporphyrinogen-III with modified side chains: Implications for binding at the active site of coproporphyrinogen oxidase. Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions...