| Structural highlights
Function
[OLYA6_PLEOS] Has hemolytic activity against bovine erythrocytes at nanomolar concentrations in vitro. Promotes active pleurotolysin B (PlyB)-dependent permeabilization of membranes rich in cholesterol and sphingomyelin. May play an important role in the initial phase of fungal fruiting.[1] [2]
Publication Abstract from PubMed
Sphingomyelin and cholesterol are essential lipids that are enriched in plasma membranes of animal cells, where they interact to regulate membrane properties and many intracellular signaling processes. Despite intense study, the interaction between these lipids in membranes is not well understood. Here, structural and biochemical analyses of ostreolysin A (OlyA), a protein that binds to membranes only when they contain both sphingomyelin and cholesterol, reveal that sphingomyelin adopts two distinct conformations in membranes when cholesterol is present. One conformation, bound by OlyA, is induced by stoichiometric, exothermic interactions with cholesterol, properties that are consistent with sphingomyelin/cholesterol complexes. In its second conformation, sphingomyelin is free from cholesterol and does not bind OlyA. A point mutation abolishes OlyA's ability to discriminate between these two conformations. In cells, levels of sphingomyelin/cholesterol complexes are held constant over a wide range of plasma membrane cholesterol concentrations, enabling precise regulation of the chemical activity of cholesterol.
Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes.,Endapally S, Frias D, Grzemska M, Gay A, Tomchick DR, Radhakrishnan A Cell. 2019 Jan 25. pii: S0092-8674(18)31656-8. doi: 10.1016/j.cell.2018.12.042. PMID:30712872[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Berne S, Krizaj I, Pohleven F, Turk T, Macek P, Sepcic K. Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting. Biochim Biophys Acta. 2002 Apr 15;1570(3):153-9. PMID:12020804
- ↑ Ota K, Leonardi A, Mikelj M, Skocaj M, Wohlschlager T, Kunzler M, Aebi M, Narat M, Krizaj I, Anderluh G, Sepcic K, Macek P. Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B. Biochimie. 2013 Oct;95(10):1855-64. doi: 10.1016/j.biochi.2013.06.012. Epub 2013 , Jun 25. PMID:23806422 doi:http://dx.doi.org/10.1016/j.biochi.2013.06.012
- ↑ Endapally S, Frias D, Grzemska M, Gay A, Tomchick DR, Radhakrishnan A. Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes. Cell. 2019 Jan 25. pii: S0092-8674(18)31656-8. doi: 10.1016/j.cell.2018.12.042. PMID:30712872 doi:http://dx.doi.org/10.1016/j.cell.2018.12.042
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