Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
| Autor: | Andreas Vogt, Albena Draycheva, Patrick Kuhn, Narcis-Adrian Petriman, Friedel Drepper, Wolfgang Wintermeyer, Hans-Georg Koch, Lukas Sturm, Bettina Warscheid |
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| Rok vydání: | 2015 |
| Předmět: |
Receptors
Peptide Receptors Cytoplasmic and Nuclear Biology medicine.disease_cause Binding Competitive environment and public health Ribosome Article Bacterial Proteins Ribosomal protein Protein targeting Escherichia coli medicine Signal recognition particle receptor Research Articles Adenosine Triphosphatases SecYEG Translocon Signal recognition particle SecA Proteins Endoplasmic reticulum membrane Escherichia coli Proteins Membrane Transport Proteins Cell Biology Translocon Lipids Biochemistry Protein Biosynthesis Biophysics Ribosomes Signal Recognition Particle SEC Translocation Channels Protein Binding |
| Zdroj: | Journal of Cell Biology The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.201502103 |
| Popis: | The cotranslational transfer of nascent membrane proteins to the SecYEG translocon is facilitated by a reorientation of the SecY-bound signal recognition particle (SRP) receptor, FtsY, which accompanies the formation of a quaternary targeting complex consisting of SecYEG, FtsY, SRP, and the ribosome. 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. |
| Databáze: | OpenAIRE |
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