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Showing 1–4 of 4 results
Advanced filters: Author: Achim Dickmanns Clear advanced filters

  • Nuclear protein homeostasis relies on proteasome import into the nucleus. Here the authors identify how assembled human proteasomes are transported across the nuclear pore complex and reveal a mechanism enabling the large complex to bypass pore size limitations.

    • Hanna L. Brunner
    • Robert W. Kalis
    • David Haselbach
    ResearchOpen Access
    Nature Communications
    P: 1-17

  • In several bacteria, cyclic di-AMP mediates potassium (K+) and osmotic homeostasis. Here, the authors show that DarB, a Bacillus subtilis protein previously reported to bind cyclic di-AMP, interacts with the (p)ppGpp synthetase/hydrolase Rel in a K+-dependent manner in turn leading to Rel-dependent accumulation of pppGpp under conditions of K+ starvation.

    • Larissa Krüger
    • Christina Herzberg
    • Jörg Stülke
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Some viral proteins involved in interaction with the host cell surface adopt a very rigid and stable triple–β-helix fold. In order to attain this complex fold, these proteins contain an intramolecular chaperone domain that is auto-cleaved after assembly. Now structural work on two such chaperone domains indicates how they can promote correct folding of the β-helices.

    • Eike C Schulz
    • Achim Dickmanns
    • Ralf Ficner
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 210-215