Protein targeting by the signal recognition particle
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Przemyslaw Grudnik
Abstract
Protein targeting by the signal recognition particle (SRP) is universally conserved and starts with the recognition of a signal sequence in the context of a translating ribosome. SRP54 and FtsY, two multidomain proteins with guanosine triphosphatase (GTPase) activity, are the central elements of the SRP system. They have to coordinate the presence of a signal sequence with the presence of a vacant translocation channel in the membrane. For coordination the two GTPases form a unique, nearly symmetric heterodimeric complex in which the activation of GTP hydrolysis plays a key role for membrane insertion of substrate proteins. Recent results are integrated in an updated perception of the order of events in SRP-mediated protein targeting.
©2009 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Guest Editorial
- Highlight: The gatekeepers of life yield their secrets
- Highlight: Membrane Transport and Communication
- First structural insights into the TpsB/Omp85 superfamily
- Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
- Structural and functional aspects of the multidrug efflux pump AcrB
- From the Sec complex to the membrane insertase YidC
- Emerging roles of mitochondrial membrane dynamics in health and disease
- Mitochondrial tRNA import – the challenge to understand has just begun
- Multiple pathways for mitochondrial protein traffic
- Challenges to our current view on chloroplasts
- Molecular interactions within the plant TOC complex
- Protein transport across the peroxisomal membrane
- On the fate of early endosomes
- ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
- Protein targeting by the signal recognition particle
- The peptide-loading complex – antigen translocation and MHC class I loading
- Protein-lipid interactions: paparazzi hunting for snap-shots
- The nanodisc: a novel tool for membrane protein studies
- NMR and EPR studies of membrane transporters