000030557 001__ 30557
000030557 005__ 20150420164423.0
000030557 0248_ $$aoai:doc.rero.ch:20121108093156-BK$$punifr$$ppostprint$$prero_explore$$particle$$zthesis_urn$$zcdu57$$zreport$$zthesis$$zbook$$zjournal$$zcdu16$$zpreprint$$zcdu1$$zdissertation$$zcdu34
000030557 041__ $$aeng
000030557 080__ $$a57
000030557 100__ $$aChoudhary, Vineet$$uDivision of Biochemistry, Department of Biology, University of Fribourg, Switzerland
000030557 245__ $$9eng$$aPathogen-Related Yeast (PRY) proteins and members of the CAP superfamily are secreted sterol-binding proteins
000030557 269__ $$c2012
000030557 520__ $$9eng$$aSterols and related membrane-perturbing agents are subject to a quality control cycle. Compounds that fail to pass this control are acetylated and secreted into the culture media, whereas lipids that pass the cycle are deacetylated and retained within the cell. Here we describe the identification of a family of conserved proteins, the Pathogen-Related Yeast (PRY) proteins, as a class of sterol-binding proteins. Saccharomyces cerevisiae has three members of this family, two of which, Pry1 and Pry2, are secreted, whereas Pry3 is a cell wall–associated protein. Cells lacking both PRY1 and PRY2 have a complete block in secretion of the acetylated lipid and Pry1 and Pry2 proteins bind free cholesterol and cholesteryl acetate in vitro. PRY proteins belong to a large protein superfamily of unknown mode of action, the CAP protein superfamily [i.e. cysteine-rich secretory proteins (CRISP), antigen 5, and pathogenesis related 1 proteins]. The conserved CAP domain of Pry1 is necessary and sufficient for lipid export and sterol binding. Expression of a human CAP superfamily member, the cysteine-rich secretory protein 2 (CRISP2), rescues the phenotype of yeast mutants lacking Pry function and purified CRISP2 binds cholesterol in vitro, indicating that lipid binding is a conserved function of the CAP superfamily proteins.
000030557 700__ $$aSchneiter, Roger$$uDivision of Biochemistry, Department of Biology, University of Fribourg, Switzerland
000030557 773__ $$g2012/109/42/16882-16887$$tProceedings of the National Academy of Sciences of the United States of America - PNAS
000030557 775__ $$gPublished version$$ohttp://dx.doi.org/10.1073/pnas.1209086109
000030557 8564_ $$fsch_pry.pdf$$qapplication/pdf$$s978884$$uhttp://doc.rero.ch/record/30557/files/sch_pry.pdf$$yorder:1$$zpdf
000030557 8564_ $$fsch_pry_sm.pdf$$qapplication/pdf$$s836791$$uhttp://doc.rero.ch/record/30557/files/sch_pry_sm.pdf$$yorder:2$$zSupplementary material
000030557 918__ $$aFaculté des sciences$$bDécanat, Ch. du Musée 6A, 1700 Fribourg$$cBiologie
000030557 919__ $$aUniversité de Fribourg$$bFribourg$$ddoc.support@rero.ch
000030557 980__ $$aPOSTPRINT$$bUNIFR$$fART_JOURNAL
000030557 990__ $$a20121108093156-BK