SecYEG activates GTPases to drive the completion of cotranslational protein targeting
Copyright policy )SecYEG activates GTPases to drive the completion of cotranslational protein targeting
Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the translating ribosome or actively regulates this targeting machinery remains unclear. Here we show that SecYEG drives conformational changes in the cargo-loaded SRP–SR targeting complex that activate it for GTP hydrolysis and for handover of the translating ribosome. These results provide the first evidence that SecYEG actively drives the efficient delivery and unloading of translating ribosomes at the target membrane.
Receptors, Peptide, Escherichia coli Proteins, Hydrolysis, 610, Receptors, Cytoplasmic and Nuclear, Models, Biological, Protein Structure, Tertiary, Protein Transport, Escherichia coli, Guanosine Triphosphate, Ribosomes, Signal Recognition Particle, Research Articles, SEC Translocation Channels
Receptors, Peptide, Escherichia coli Proteins, Hydrolysis, 610, Receptors, Cytoplasmic and Nuclear, Models, Biological, Protein Structure, Tertiary, Protein Transport, Escherichia coli, Guanosine Triphosphate, Ribosomes, Signal Recognition Particle, Research Articles, SEC Translocation Channels
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