The signal recognition particle and its interactions during protein targeting |
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Authors: | Halic Mario Beckmann Roland |
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Affiliation: | 1. Department of Biology, Stanford University, Stanford, CA 94305, USA;2. Biophysics Program, Stanford University, Stanford, CA 94305, USA;3. Department of Genetics, Stanford University, Stanford, CA 94305, USA |
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Abstract: | The synthesis of secretory or integral membrane proteins can be directly coupled to their translocation across or insertion into membranes. In co-translational targeting, the translation machine, the ribosome, is transferred to the respective membrane by the signal recognition particle (SRP) and its receptor (SR) as soon as a signal sequence emerges. Protein synthesis can continue at the membrane, with the nascent peptide chain directly inserting into the ribosome-bound protein-conducting channel, the Sec61 complex. During the past two years, several structures have been solved by crystallography and cryo-electron microscopy that represent distinct functional states of the SRP cycle. On this basis, the first structure-based models can be suggested that explain important aspects of protein targeting, such as the SRP-ribosome and SRP-SR interactions. |
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