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Roles of the pH signaling transcription factor PacC in Wangiella (Exophiala) dermatitidis.


ABSTRACT: To study the function of the PacC transcription factor in Wangiella dermatitidis, a black, polymorphic fungal pathogen of humans with yeast-phase predominance, the PACC gene was cloned, sequenced, disrupted and expressed. Three zinc finger DNA-binding motifs were found at the N-terminus, and a signaling protease cleavage site at the C-terminus. PACC was more expressed at neutral-alkaline pH than at acidic pH. Truncation at about 40 residues of the coding sequence upstream of the conserved protease processing cleavage site of PacC affected growth on a nutrient-rich medium, increased sensitivity to Na(+) stress, decreased yeast growth at neutral-alkaline pH, and repressed hyphal growth on a nutrient-poor medium at 25 degrees C. Truncation at the coding sequence for the conserved signaling protease box of PacC impaired growth and reduced RNA expression of the class II chitin synthase gene at acidic pH. The results suggested that PacC is important not only for the adaptation of W. dermatitidis to different ambient pH conditions and Na(+) stress conditions, but also for influencing yeast-hyphal transitions in this agent of phaeohyphomycosis.

SUBMITTER: Wang Q 

PROVIDER: S-EPMC2755521 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Roles of the pH signaling transcription factor PacC in Wangiella (Exophiala) dermatitidis.

Wang Qin Q   Szaniszlo Paul J PJ  

Fungal genetics and biology : FG & B 20090606 9


To study the function of the PacC transcription factor in Wangiella dermatitidis, a black, polymorphic fungal pathogen of humans with yeast-phase predominance, the PACC gene was cloned, sequenced, disrupted and expressed. Three zinc finger DNA-binding motifs were found at the N-terminus, and a signaling protease cleavage site at the C-terminus. PACC was more expressed at neutral-alkaline pH than at acidic pH. Truncation at about 40 residues of the coding sequence upstream of the conserved protea  ...[more]

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