We studied the cellular localization of the archaeal exosome, an RNA-processing protein complex containing orthologs of the eukaryotic proteins Rrp41, Rrp42, Rrp4 and Csl4, and an archaea-specific subunit annotated as DnaG. Fractionation of cell-free extracts of Sulfolobus solfataricus in sucrose density gradients revealed that DnaG and the active-site comprising subunit Rrp41 are enriched together with surface layer proteins in a yellow colored ring, implicating that the exosome is membrane-bound. In accordance with this assumption, DnaG and Rrp41 were detected at the periphery of the cell by immunofluorescence microscopy. Our finding suggests that RNA processing in Archaea is spatially organized. Structured summary: MINT-7891213: Rrp41 (uniprotkb:. Q9UXC2) and DnaG (uniprotkb:. P95980) colocalize (MI:. 0403) by cosedimentation in solution (MI:. 0028). MINT-7891235: Rrp41 (uniprotkb:. Q9UXC2), DnaG (uniprotkb:. P95980) and SlaA (uniprotkb:. Q2M1E7) colocalize (MI:. 0403) by cosedimentation through density gradient (MI:. 0029). MINT-7891278: Rrp41 (uniprotkb:. Q9UXC2) and DnaG (uniprotkb:. P95980) colocalize (MI:. 0403) by fluorescence microscopy (MI:. 0416). © 2010 Federation of European Biochemical Societies.
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