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Journal Article

Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.

MPS-Authors
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Draycheva,  A.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

2183348.pdf
(Publisher version), 4MB

Supplementary Material (public)

2183348_Suppl.pdf
(Supplementary material), 550KB

Citation

Kuhn, P., Draycheva, A., Vogt, A., Petriman, N. A., Sturm, L., Drepper, F., et al. (2015). Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. Journal of Cell Biology, 211(1), 91-104. doi:10.1083/jcb.201502103.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-4664-F
Abstract
Cotranslational protein targeting delivers proteins to the bacterial cytoplasmic membrane or to the eukaryotic endoplasmic reticulum membrane. The signal recognition particle (SRP) binds to signal sequences emerging from the ribosomal tunnel and targets the ribosome-nascent-chain complex (RNC) to the SRP receptor, termed FtsY in bacteria. FtsY interacts with the fifth cytosolic loop of SecY in the SecYEG translocon, but the functional role of the interaction is unclear. By using photo-cross-linking and fluorescence resonance energy transfer measurements, we show that FtsY–SecY complex formation is guanosine triphosphate independent but requires a phospholipid environment. Binding of an SRP–RNC complex exposing a hydrophobic transmembrane segment induces a rearrangement of the SecY–FtsY complex, which allows the subsequent contact between SecY and ribosomal protein uL23. These results suggest that direct RNC transfer to the translocon is guided by the interaction between SRP and translocon-bound FtsY in a quaternary targeting complex.