Chaperone binding at the ribosomal exit tunnel
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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.
Originalsprog | Engelsk |
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Tidsskrift | Structure |
Vol/bind | 11 |
Udgave nummer | 12 |
Sider (fra-til) | 1547-56 |
Antal sider | 10 |
ISSN | 0969-2126 |
Status | Udgivet - 2003 |
ID: 40318630