Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites

@article{Angelini2006MembraneBO,
  title={Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites},
  author={Sandra Angelini and Diana Boy and E. Schiltz and H. Koch},
  journal={The Journal of Cell Biology},
  year={2006},
  volume={174},
  pages={715 - 724}
}
  • Sandra Angelini, Diana Boy, +1 author H. Koch
  • Published 2006
  • Biology, Medicine
  • The Journal of Cell Biology
  • Cotranslational protein targeting in bacteria is mediated by the signal recognition particle (SRP) and FtsY, the bacterial SRP receptor (SR). FtsY is homologous to the SRα subunit of eukaryotes, which is tethered to the membrane via its interaction with the membrane-integral SRβ subunit. Despite the lack of a membrane-anchoring subunit, 30% of FtsY in Escherichia coli are found stably associated with the cytoplasmic membrane. However, the mechanisms that are involved in this membrane… CONTINUE READING
    Signal recognition particle: an essential protein-targeting machine.
    • 240
    • PDF
    The Sec translocase.
    • 189
    • PDF
    Protein targeting by the signal recognition particle
    • 134
    • PDF
    How translocons select transmembrane helices.
    • 182
    • PDF
    The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
    • 62

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 56 REFERENCES
    X-ray structure of a protein-conducting channel
    • 1,107
    • PDF
    SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • 545
    • Highly Influential
    Protein translocation across the endoplasmic reticulum
    • 563
    The Escherichia coli SRP and SecB targeting pathways converge at the translocon
    • 296
    • PDF