PMID:16299512
| Citation |
Spanggord, RJ, Siu, F, Ke, A and Doudna, JA (2005) RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle. Nat. Struct. Mol. Biol. 12:1116-22 |
|---|---|
| Abstract |
The signal recognition particle (SRP) targets nascent proteins to cellular membranes for insertion or secretion by recognizing polypeptides containing an N-terminal signal sequence as they emerge from the ribosome. GTP-dependent binding of SRP to its receptor protein leads to controlled release of the nascent chain into a membrane-spanning translocon pore. Here we show that the association of the SRP with its receptor triggers a marked conformational change in the complex, localizing the SRP RNA and the adjacent signal peptide-binding site at the SRP-receptor heterodimer interface. The orientation of the RNA suggests how peptide binding and GTP hydrolysis can be coupled through direct structural contact during cycles of SRP-directed protein translocation. |
| Links |
PubMed Online version:10.1038/nsmb1025 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Dimerization; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/metabolism; Guanosine Triphosphate/metabolism; Hydrolysis; Peptides/metabolism; Protein Conformation; Protein Structure, Tertiary; RNA, Bacterial; RNA, Ribosomal/chemistry; RNA, Ribosomal/metabolism; Receptors, Cytoplasmic and Nuclear/chemistry; Receptors, Cytoplasmic and Nuclear/metabolism; Receptors, Peptide/chemistry; Receptors, Peptide/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/metabolism |
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