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Roppelt V.,Institute For Mikrobiologie Und Molekularbiologie Der Jlu Giessen | Hobel C.F.V.,Max Planck Institute For Entwicklungsbiologie | Albers S.V.,Max Planck Institute For Terrestrische Mikrobiologie | Lassek C.,Institute For Mikrobiologie Und Molekularbiologie Der Jlu Giessen | And 3 more authors.
FEBS Letters | Year: 2010

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. Source


Roppelt V.,Institute For Mikrobiologie Und Molekularbiologie Der Jlu Giessen | Klug G.,Institute For Mikrobiologie Und Molekularbiologie Der Jlu Giessen | Evguenieva-Hackenberg E.,Institute For Mikrobiologie Und Molekularbiologie Der Jlu Giessen
FEBS Letters | Year: 2010

We studied the substrate specificity of the exosome of Sulfolobus solfataricus using the catalytically active Rrp41-Rrp42-hexamer and complexes containing the RNA-binding subunits Rrp4 or Csl4. The conservation of both Rrp4 and Csl4 in archaeal and eukaryotic exosomes suggests specific functions for each of them. We found that they confer different specificities to the exosome: RNA with an A-poor 3'-end is degraded with higher efficiency by the Csl4-exosome, while the Rrp4-exosome strongly prefers poly(A)-RNA. High C-content and polyuridylation negatively influence RNA processing by all complexes, and, in contrast to the hexamer, the Rrp4-exosome prefers longer substrates. © 2010 Federation of European Biochemical Societies. Source

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