“L23 Protein Functions as a Chaperone Docking Site on the Ribosome”

10/23/02


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Table of Contents

“L23 Protein Functions as a Chaperone Docking Site on the Ribosome”

Overview

Chaperones and Folding

Chaperone Pathway in Bacteria

Trigger Factor (TF)

Significance

A Few Questions

TF Signature

TF Signature and Mutants

TF Signature Mutants

FRK/AAA Mutant Association with Ribosomes

FRK/AAA Mutant Association with Ribosomes

TF Signature Mutants

D42C Mutant Association and Crosslinking with Ribosomes

D42C Mutant Association and Crosslinking with Ribosomes

Interaction is Specific

L23 and L29

L23 and L29 Deletion Mutants

L23 and L29 Deletion Mutants

L23 and L29 Deletion Mutants

L29 and TF Binding

TF Remains Associated to L29-Deficient Ribosomes

TF Can Rebind to L29-Deficient Ribosomes

L23 Deletion and Mutants

L23 Region 1 and 2 Mutants

L23 Region 1 and 2 Mutants

L23 Mutants and TF Binding

L23 Mutants and TF Binding

L23 Mutants and TF Binding

L23 Mutants and TF Binding

TF Interacts Directly with L23

TF Interacts Directly with L23

TF • Nascent Polypeptide Interaction and L23

In Vitro Transcription/ Translation System

Crosslinking

Identifying Crosslink Results

L23 is Required for TF • ICDH Interaction

TF-Ribosome Interaction and In Vivo Protein Folding

TF-Ribosome Interaction and in vivo Protein Folding

TF-Ribosome Interaction and in vivo Protein Folding

The Big Picture

Conclusions

Future Directions

Author: Anthony S. Serianni

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