L23 protein functions as a chaperone docking site on the ribosome

Günter Kramer, Thomas Rauch, Wolfgang Rist, Sonja Vorderwülbecke, Holger Patzelt, Agnes Schulze-Specking, Nenad Ban, Elke Deuerling () and Bernd Bukau ()
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Günter Kramer: Universität Freiburg
Thomas Rauch: Universität Freiburg
Wolfgang Rist: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282
Sonja Vorderwülbecke: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282
Holger Patzelt: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282
Agnes Schulze-Specking: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282
Nenad Ban: Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology, ETH Hönggerberg, HPK Building
Elke Deuerling: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282
Bernd Bukau: Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, INF282

Nature, 2002, vol. 419, issue 6903, 171-174

Abstract: Abstract During translation, the first encounter of nascent polypeptides is with the ribosome-associated chaperones that assist the folding process—a principle that seems to be conserved in evolution1,2,3. In Escherichia coli, the ribosome-bound Trigger Factor chaperones the folding of cytosolic proteins by interacting with nascent polypeptides4,5. Here we identify a ribosome-binding motif in the amino-terminal domain of Trigger Factor. We also show the formation of crosslinked products between Trigger Factor and two adjacent ribosomal proteins, L23 and L29, which are located at the exit of the peptide tunnel in the ribosome. L23 is essential for the growth of E. coli and the association of Trigger Factor with the ribosome, whereas L29 is dispensable in both processes. Mutation of an exposed glutamate in L23 prevents Trigger Factor from interacting with ribosomes and nascent chains, and causes protein aggregation and conditional lethality in cells that lack the protein repair function of the DnaK chaperone. Purified L23 also interacts specifically with Trigger Factor in vitro. We conclude that essential L23 provides a chaperone docking site on ribosomes that directly links protein biosynthesis with chaperone-assisted protein folding.

Date: 2002
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DOI: 10.1038/nature01047

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