Cholesterol-Binding by the Yeast CAP Family Member Pry1 Requires the Presence of an Aliphatic Side Chain on Cholesterol
| Autor: | Roger Schneiter, Rabih Darwiche |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification biology Cholesterol binding Saccharomyces cerevisiae biology.organism_classification Ligand (biochemistry) Yeast Sterol Amino acid 03 medical and health sciences 030104 developmental biology chemistry Biochemistry Sterol binding Cyclase-associated protein family |
| Zdroj: | Journal of Steroids & Hormonal Science. 7 |
| ISSN: | 2157-7536 |
| DOI: | 10.4172/2157-7536.1000172 |
| Popis: | Pathogen-related yeast protein 1 (Pry1) is a Saccharomyces cerevisiae member of the CAP/SCP/TAPS superfamily. Although, CAP proteins have been proposed to be implicated in a number of physiological processes, such as pathogen virulence, sperm maturation and fertilization, host-pathogen interactions and defense mechanisms, the molecular mode of action of these proteins is poorly understood. CAP proteins are mostly secreted and they are stable in the extracellular space over a wide a range of conditions. All members of this superfamily contain a common CAP domain of approximately 150 amino acids, which adopts a unique α-β-α sandwich fold. We have previously shown that the yeast CAP family members act as sterol-binding and -export proteins in vivo and that the Pry proteins bind cholesterol and cholesteryl acetate in vitro. The conserved CAP domain of Pry1 is necessary and sufficient for sterol binding. Based on these observations, it is conceivable that CAP proteins exert their biological function through a common mechanism, such as binding and sequestration of sterols or related small hydrophobic compounds. Here we analyze the ligand specificity of Pry1 in more detail and show that the presence of the aliphatic isooctane side chain of the sterol but not the 3-hydroxyl group is important for binding to Pry1. |
| Databáze: | OpenAIRE |
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