The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction

This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 Å, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of w...

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Bibliographic Details
Published in:	Structure (London) Vol. 13; no. 11; pp. 1685 - 1694
Main Authors:	Schlünzen, Frank, Wilson, Daniel N., Tian, Pingsheng, Harms, Jörg M., McInnes, Stuart J., Hansen, Harly A.S., Albrecht, Renate, Buerger, Jörg, Wilbanks, Sigurd M., Fucini, Paola
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01-11-2005
Subjects:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - physiology Binding Sites Deinococcus - chemistry Deinococcus - genetics Deinococcus - physiology Hydrophobic and Hydrophilic Interactions Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecular Chaperones - physiology Molecular Sequence Data Peptides - chemistry Peptides - metabolism Peptides - physiology Protein Binding Protein Folding Protein Structure, Tertiary Ribosomal Proteins - chemistry Ribosomal Proteins - metabolism Ribosomal Proteins - physiology Signal Recognition Particle - chemistry Signal Recognition Particle - metabolism Signal Recognition Particle - physiology
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Summary:	This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 Å, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The β hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0969-2126 1878-4186
DOI:	10.1016/j.str.2005.08.007