Identification and characterization of a functional Candida albicans homolog of the Saccharomyces cerevisiae TCO89 gene

Authors

  • Changlong Zheng,

    1. Laboratory of Molecular Microbiology, Department of Molecular and Cellular Pharmacology, College of Pharmaceuticals and Biotechnology, Tianjin University, Tianjin, China
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  • Zhihui Yan,

    1. Laboratory of Molecular Microbiology, Department of Molecular and Cellular Pharmacology, College of Pharmaceuticals and Biotechnology, Tianjin University, Tianjin, China
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  • Wei Liu,

    1. Laboratory of Molecular Microbiology, Department of Molecular and Cellular Pharmacology, College of Pharmaceuticals and Biotechnology, Tianjin University, Tianjin, China
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  • Linghuo Jiang

    1. Laboratory of Molecular Microbiology, Department of Molecular and Cellular Pharmacology, College of Pharmaceuticals and Biotechnology, Tianjin University, Tianjin, China
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  • Editor: Richard Calderone

Correspondence: Linghuo Jiang, Department of Molecular and Cellular Pharmacology, College of Pharmaceuticals and Biotechnology, Tianjin University, Tianjin, China 300072. Tel.: +86 22 2740 2527; fax: +86 22 2740 1248; e-mail: linghuojiang@yahoo.com.cn

Abstract

As one of the components of target of rapamycin complex 1 (TORC1), ScTco89p is involved in rapamycin sensitivity and cellular integrity in Saccharomyces cerevisiae. Here we provide evidence showing that deletion of ScTCO89 causes yeast cells to be hypersensitive to salt stress in a high osmolarity glycerol pathway-independent fashion. In addition, we have identified and characterized a functional Candida albicans homolog (CaTCO89) of ScTCO89, which encodes a protein of 708 amino acids that shows overall 15% identity with ScTco89p at the amino acid level. However, CaTCO89 could complement the functions of ScTCO89 in rapamycin sensitivity, salt tolerance, and cellular integrity. Candida albicans cells disrupted for CaTCO89 are also sensitive to rapamycin and lithium salt, but not susceptible to challenges to cellular integrity.

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