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Trigger factor forms a protective shield for nascent polypeptides at the ribosome.

Anja Hoffmann1, Frieder Merz, Anna Rutkowska

  • 1Zentrum für Molekulare Biologie Heidelberg (ZMBH), Im Neuenheimer Feld 282, Universität Heidelberg, 69120 Heidelberg, Germany.

The Journal of Biological Chemistry
|January 13, 2006
PubMed
Summary

Trigger Factor (TF) protects newly synthesized proteins from degradation by shielding unfolded polypeptides emerging from the ribosome. This chaperone function is crucial for de novo protein folding and preventing aggregation.

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Area of Science:

  • Molecular Biology
  • Protein Folding
  • Chaperone Proteins

Background:

  • Ribosome-associated Trigger Factor (TF) is the initial chaperone encountered by nascent polypeptides.
  • The precise role of TF in shielding polypeptides at the ribosome remains incompletely understood.

Purpose of the Study:

  • To investigate the capacity of TF to shield nascent polypeptides emerging from the ribosomal exit tunnel.
  • To determine the impact of TF on the stability and degradation of unfolded nascent proteins.

Main Methods:

  • Synthesized arrested nascent polypeptides of varying sizes and folding statuses using an in vitro transcription/translation system.
  • Assessed polypeptide degradation by proteinase K in the presence and absence of TF and its variants.
  • Compared the protective efficacy of ribosome-tethered TF with non-ribosomal TF and the DnaK system.

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Main Results:

  • Unfolded nascent polypeptides were rapidly degraded without TF, unless folded into a compact domain.
  • TF, and a fragment lacking its peptidyl-prolyl isomerase domain, protected all tested unfolded nascent polypeptides from degradation.
  • Ribosome-tethered TF provided specific protection, outperforming non-ribosomal TF and the DnaK system.
  • TF shielded large nascent polypeptides (up to 41 kDa), indicating a broad protective capability.

Conclusions:

  • TF shields nascent polypeptides on the ribosome, preventing degradation and aggregation.
  • This shielding mechanism supports productive de novo protein folding, especially for large multidomain proteins.
  • TF's ribosome-tethered protective function is critical for efficient protein biogenesis in prokaryotes.