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Evidence for involvement of two naphthol reductases in the first reduction step of melanin biosynthesis pathway of Colletotrichum lagenarium

Published online by Cambridge University Press:  12 August 2003

Gento TSUJI ,
Tomomi SUGAHARA ,
Isáo FUJII ,
Yuichiro MORI ,
Yutaka EBIZUKA ,
Tomonori SHIRAISHI  and
Yasuyuki KUBO
Gento TSUJI
Affiliation:
Laboratory of Plant Pathology, Graduate School of Agriculture, Kyoto Prefectural University, Kyoto 606-8522, Japan. E-mail: [email protected] Laboratory of Plant Pathology and Genetic Engineering, Faculty of Agriculture, Okayama University, Okayama 700-8530, Japan.
Tomomi SUGAHARA
Affiliation:
Laboratory of Plant Pathology, Graduate School of Agriculture, Kyoto Prefectural University, Kyoto 606-8522, Japan. E-mail: [email protected]
Isáo FUJII
Affiliation:
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Yuichiro MORI
Affiliation:
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Yutaka EBIZUKA
Affiliation:
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Tomonori SHIRAISHI
Affiliation:
Laboratory of Plant Pathology and Genetic Engineering, Faculty of Agriculture, Okayama University, Okayama 700-8530, Japan.
Yasuyuki KUBO
Affiliation:
Laboratory of Plant Pathology, Graduate School of Agriculture, Kyoto Prefectural University, Kyoto 606-8522, Japan. E-mail: [email protected]
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Abstract

Colletotrichum lagenarium is a plant pathogenic fungus, and produces melanin that is an essential factor for appressorial penetration into host tissues. The melanin biosynthesis pathway of C. lagenarium starts with pentaketide synthesis catalyzed by polyketide synthase Pks1p. We previously confirmed that the direct product of Pks1p is 1,3,6,8-tetrahydroxynaphthalene. Thus, melanin biosynthesis in this fungus requires the reduction of 1,3,6,8-tetrahydroxynaphthalene to scytalone. We made a double mutant 9141-144 from the thr1 mutant 9141 that lacks the ability to metabolize 1,3,8-trihydroxynaphthalene. The double mutant 9141-144 could metabolize neither 1,3,6,8-tetrahydroxynaphthalene nor 1,3,8-trihydroxynaphthalene. However melanin production by the double mutant was restored by THR1, indicating that Thr1p can metabolize both compounds in vivo. These results demonstrate that two enzymes, Thr1p and a deduced 1,3,6,8-tetrahydroxynaphthalene-specific reductase, are involved in the first reduction step of the melanin biosynthesis pathway of C. lagenarium.

Type
Research Article
Information
Mycological Research , Volume 107 , Issue 7 , July 2003 , pp. 854 - 860
Copyright
© The British Mycological Society 2003

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