Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains

Stephan   N.   Witt

doi:10.2174/092986609788490195

Abstract

This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 Å from the emerging nascent chain has an effective concentration of 1 x 10 M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10 s in order to keep chains unfolded.

Keywords: Chaperone, holdase, kinetic partitioning, proximity effect, ribosome-associated chaperone

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Protein & Peptide Letters

Title: Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains

Volume: 16 Issue: 6

Author(s): Stephan N. Witt

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Keywords: Chaperone, holdase, kinetic partitioning, proximity effect, ribosome-associated chaperone

Abstract: This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 Å from the emerging nascent chain has an effective concentration of 1 x 10 M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10 s in order to keep chains unfolded.

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Witt N. Stephan, Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains, Protein & Peptide Letters 2009; 16 (6) . https://dx.doi.org/10.2174/092986609788490195