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The compartmentalization of melanin biosynthetic enzymes Contributes to self-defense against intermediate compound scytalone in Botrytis cinerea

Xue Chen  Yantao Na  Pinkuan Zhu  Yiwen Wang  Yina Jiang  Yifan He  Chenghua Zhang  Dandan Ren  Han Guo  Sheng Xiang  Qin Li  Ling Xu  
【摘要】:In filamentous fungi, 1,8-dihydroxynaphthalene(DHN) melanin is a major component of the extracellular matrix, endowing fungi with environmental tolerance, and some pathogenic species with pathogenicity. However, the cytological mechanism of the melanin biosynthesis pathway remains obscure. Using the gray mold pathogen Botrytis cinerea, six key enzymes participate in DHN melanin synthesis, including polyketide synthases Bc PKS12/13, hydrolase Bc YGH1, 1,3,6,8-tetrahydroxynaphthalene(THN) reductases BcBRN1/2, and scytalone dehydratase Bc SCD1. We identified that the ?bcscd1 mutant accumulated scytalone in culture filtrate rather than in mycelium. Excessive scytalone appears to be self-toxic to the fungus, leading to repressed sclerotial germination and sporulation in the ?bcscd1 mutant. The BcBRN1/2 enzymes responsible for synthesizing scytalone were localized in endosomes and further trafficked to the cell surface. The BcSCD1 accumulated on the cell wall, being consistent with extracellular occurrence of its precursor scytalone. Moreover, the early stage melanin synthesis enzymes, including the BcPKS12/13 and BcYGH1, were localized in peroxisome vesicles. This study revealed the sub-cellular mechanisms of melanin biosynthetic enzymes in B. cinerea, indicating that encapsulation and externalization of the melanin synthetic enzymes should be harmoniously organized, most likely to assure enzymatic efficiency, and to avoid the adverse effect of the intermediate.

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