Abstract：
:Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During ongoing synthesis, nascent protein chains are particularly sensitive to aggregation and degradation because they emerge from the ribosome in an unfolded state. In bacteria, the first protein to interact with nascent chains and facilitate their folding is the ribosome-associated chaperone trigger factor. Recently, crystal structures of trigger factor and of its ribosome-binding domain in complex with the large ribosomal subunit revealed that the chaperone adopts an extended 'dragon-shaped' fold with a large hydrophobic cradle, which arches over the exit of the ribosomal tunnel and shields newly synthesized proteins. These structural results, together with recent biochemical data on trigger factor and its interplay with other chaperones and factors that interact with the nascent chain, provide a comprehensive view of the role of trigger factor during co-translational protein folding.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Maier T,Ferbitz L,Deuerling E,Ban Ndoi
10.1016/j.sbi.2005.03.005subject
Has Abstractpub_date
2005-04-01 00:00:00pages
204-12issue
2eissn
0959-440Xissn
1879-033Xpii
S0959-440X(05)00056-4journal_volume
15pub_type
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