Research Article

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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Science  09 May 2014:
Vol. 344, Issue 6184, 1250494
DOI: 10.1126/science.1250494

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Molecular chaperones play a key role in maintaining protein homeostasis in the cell by preventing protein aggregation and misfolding. Chaperone-substrate complexes tend to be large and dynamic, making structure determination challenging. Saio et al. (10.1126/science.1250494; see the Perspective by Gamerdinger and Deuerling) used advanced NMR spectroscopy techniques to determine the structure of three trigger factor (TF) chaperone molecules in complex with the unfolded substrate, alkaline phosphatase (PhoA), and of each of the TFs in complex with the relevant region of PhoA. TF binds at multiple sites on PhoA through hydrophobic contacts, thus shielding these residues from solvent and preventing aggregation. The stability of the complex increases as longer PhoA regions are engaged by TF, and the multivalent binding keeps the substrate in an extended conformation.

  • * These authors contributed equally to this work.

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