Journal of Biological Chemistry · 2006 · 32 citations · 43 references
Life SciencesBiologyMolecular BiologyMolecular RecognitionProtein FoldingProtein TranslationProtein SynthesisProtein TargetingRibosome BiogenesisRibosome FunctionTranslation In EukaryotesTranslation In ProkaryotesDownstream Sequence ElementsRibosomal RnasRibosome-associated ChaperonesSec Translocon PathwaySignal Peptide MotifSignal Peptide-mediated TargetingSignal PeptidesSignal Recognition Particle Targeting
Different from cytoplasmic membrane proteins, presecretory proteins of bacteria usually do not require the signal recognition particle for targeting to the Sec translocon. Nevertheless signal sequences of presecretory proteins have been found in close proximity to signal recognition particle immediately after they have emerged from the ribosome. We show here that at the ribosome, the molecular environment of a signal sequence depends on the nature of downstream sequence elements that can cause an alternate recruitment of signal recognition particle and the ribosome-associated chaperone Trigger factor to a growing nascent chain. While signal recognition particle and Trigger factor might remain bound to the same ribosome, both ligands are clearly able to displace each other from a nascent chain. The data also imply that a signal sequence owes its molecular environment to the fact that it remains closely apposed to the ribosomal exit site during growth of a nascent secretory protein.
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