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

FEMS Yeast Res. 2007 Jun;7(4):558-68. doi: 10.1111/j.1567-1364.2007.00210.x. Epub 2007 Feb 9.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Candida albicans / genetics*
  • Candida albicans / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Gene Deletion
  • Lithium Compounds / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Sirolimus / metabolism

Substances

  • Fungal Proteins
  • Lithium Compounds
  • Saccharomyces cerevisiae Proteins
  • Tco89 protein, S cerevisiae
  • Sirolimus