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Updated: Jul 11, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Binding specificity of Escherichia coli trigger factor.

H Patzelt¹, S Rüdiger, D Brehmer

¹Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.

Proceedings of the National Academy of Sciences of the United States of America

|November 29, 2001

Summary

This summary is machine-generated.

Trigger factor (TF) binds specific peptide motifs on nascent proteins. Ribosome association is crucial for TF

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Area of Science:

Molecular Biology
Protein Folding
Chaperone Proteins

Background:

Trigger factor (TF) is a ribosome-associated chaperone in E. coli.
TF assists in the folding of newly synthesized cytosolic proteins.

Purpose of the Study:

To determine the substrate specificity of TF.
To investigate the binding mechanism and interaction site of TF with nascent polypeptides.

Main Methods:

Screening of 2842 membrane-coupled 13-meric peptides for TF binding.
Fluorescence spectroscopy to analyze peptide binding in solution.
Crosslinking experiments with TF fragments.
Homology modeling of the TF peptidyl-prolyl cis/trans isomerase (PPIase) domain.

Main Results:

TF binding motif identified as an 8-amino acid stretch rich in basic/aromatic residues with positive net charge.
TF shows similar substrate specificity in solution, but requires ribosome association for high affinity.
Binding occurs via the PPIase domain, independent of prolyl residues.
A mutated PPIase domain (E178V) enhanced TF association with peptides.

Conclusions:

TF recognizes specific substrate motifs on nascent polypeptides.
Ribosome association is essential for efficient TF function in vivo.
The PPIase domain's binding pocket, featuring aromatic residues and negative charge, dictates substrate specificity.
Both prolyl-independent binding and peptidyl-prolyl isomerization likely involve the same TF binding site.