Journal article

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Pathogen-Related Yeast (PRY) proteins and members of the CAP superfamily are secreted sterol-binding proteins

  • Choudhary, Vineet Division of Biochemistry, Department of Biology, University of Fribourg, Switzerland
  • Schneiter, Roger Division of Biochemistry, Department of Biology, University of Fribourg, Switzerland
    2012
Published in:
  • Proceedings of the National Academy of Sciences. - 2012, vol. 109, no. 42, p. 16882-16887
English Sterols and related membrane-perturbing agents are subject to a quality control cycle. Compounds that fail to pass this control are acetylated and secreted into the culture media, whereas lipids that pass the cycle are deacetylated and retained within the cell. Here we describe the identification of a family of conserved proteins, the Pathogen-Related Yeast (PRY) proteins, as a class of sterol-binding proteins. Saccharomyces cerevisiae has three members of this family, two of which, Pry1 and Pry2, are secreted, whereas Pry3 is a cell wall–associated protein. Cells lacking both PRY1 and PRY2 have a complete block in secretion of the acetylated lipid and Pry1 and Pry2 proteins bind free cholesterol and cholesteryl acetate in vitro. PRY proteins belong to a large protein superfamily of unknown mode of action, the CAP protein superfamily [i.e. cysteine-rich secretory proteins (CRISP), antigen 5, and pathogenesis related 1 proteins]. The conserved CAP domain of Pry1 is necessary and sufficient for lipid export and sterol binding. Expression of a human CAP superfamily member, the cysteine-rich secretory protein 2 (CRISP2), rescues the phenotype of yeast mutants lacking Pry function and purified CRISP2 binds cholesterol in vitro, indicating that lipid binding is a conserved function of the CAP superfamily proteins.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/302569
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