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Proteomic analysis of secreted membrane vesicles of Archaeal Sulfolobus species reveals the presence of endosome sorting complex components

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Ellen,  A.
Max Planck Research Group Molecular Biology of Archaea, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Albers,  S.
Max Planck Research Group Molecular Biology of Archaea, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Ellen, A., Albers, S., Huibers, W., Pitcher, A., Hobel, C., Schwarz, H., et al. (2009). Proteomic analysis of secreted membrane vesicles of Archaeal Sulfolobus species reveals the presence of endosome sorting complex components. Extremophiles, 13, 67-79.


Cite as: http://hdl.handle.net/21.11116/0000-0007-C425-2
Abstract
The crenarchaea Sulfolobus acidocaldarius, S. solfataricus and S. tokodaii, release membrane vesicles into the medium. These membrane vesicles consist of tetraether lipids and are coated with an S-layer. A proteomic analysis reveals the presence of proteins homologous to subunits of the eukaryotic endosomal sorting complex required for transport (ESCRT). Immunodetection of one of these homologs suggest a cell surface localization in intact cells. These data suggest that the membrane vesicles in Sulfolobus sp. emerge from a specific budding process with similarity to the endosomal sorting pathway.