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The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction
Author(s) -
Fucini Paola,
Schluenzen Frank,
Wilson Daniel N,
Tian Pingsheng,
Harms Joerg M.,
McKinnes Stuart,
Hansen Harley,
Albrecht Renate,
Buerger Joerg,
Wilbanks Sigurd
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a965-d
Subject(s) - ribosome , ribosomal protein , ribosomal rna , signal recognition particle , biology , folding (dsp implementation) , computational biology , genetics , biophysics , microbiology and biotechnology , chemistry , rna , gene , electrical engineering , engineering
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 to those found previously for an 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 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.