Chaperone binding at the ribosomal exit tunnel
Research output: Contribution to journal › Journal article › Research › peer-review
The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.
|Number of pages||10|
|Publication status||Published - 2003|
- Amino Acid Motifs, Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Peptidylprolyl Isomerase, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Ribosomes, Sequence Homology, Amino Acid, Signal Recognition Particle