• 제목/요약/키워드: Cryphonectria parasitica

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Identification of a Polyketide Synthase Gene in the Synthesis of Phleichrome of the Phytopathogenic Fungus Cladosporium phlei

  • So, Kum-Kang;Chung, Yun-Jo;Kim, Jung-Mi;Kim, Beom-Tae;Park, Seung-Moon;Kim, Dae-Hyuk
    • Molecules and Cells
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    • 제38권12호
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    • pp.1105-1110
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    • 2015
  • Phleichrome, a pigment produced by the phytopathogenic fungus Cladosporium phlei, is a fungal perylenequinone whose photodynamic activity has been studied intensively. To determine the biological function of phleichrome and to engineer a strain with enhanced production of phleichrome, we identified the gene responsible for the synthesis of phleichrome. Structural comparison of phleichrome with other fungal perylenequinones suggested that phleichrome is synthesized via polyketide pathway. We recently identified four different polyketide synthase (PKS) genes encompassing three major clades of fungal PKSs that differ with respect to reducing conditions for the polyketide product. Based on in silico analysis of cloned genes, we hypothesized that the non-reducing PKS gene, Cppks1, is involved in phleichrome biosynthesis. Increased accumulation of Cppks1 transcript was observed in response to supplementation with the application of synthetic inducer cyclo-(${_L}-Pro-{_L}-Phe$). In addition, heterologous expression of the Cppks1 gene in Cryphonectria parasitica resulted in the production of phleichrome. These results provide convincing evidence that the Cppks1 gene is responsible for the biosynthesis of phleichrome.

Penicillium oxalicum HCLF-34로부터 Acid Proteinase의 부분유전자 Cloning 및 Sequencing (Cloning and Sequencing of Gene Fragment of Acid Proteinase from Penicillium oxalicum HCLF-34)

  • 현성희;천재순;강상순;김진규
    • 미생물학회지
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    • 제40권1호
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    • pp.12-16
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    • 2004
  • Acid proteinase는Aspergillus niger (acid pretense A)와 Cryphonectria parasitica (acid proteinase EapC)에서 분비하는 단백질로서 치즈를 제조할 때 이용하는 단백질이다. 본 연구에서는 Penicillium oxalicum HCLF-34로부터 acid proteinase의 부분유전자를 기존에 밝혀진 acid proteinase의 homology 정보로부터 degenerate primer를 제작하여 PCR방법을 이용하여 cloning하였다. Cloning된 유전자로부터 438 bp 염기서열을 분석하였으며, 이 염기서 열을 146개의 아미노산 정보로 변환하여 acid proteinase family와 homology를 비교한 결과 acid protease A와 71% 아미노산 서열의 homology를 나타내었고, EapC와 67%의 아미노산 서열 homology가 확인되었다.