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Micro 201
Yuan Lecture 2, Class 24: Protein Folding and Molecular Chaperones
April 20th, 2017
Overview
The intracellular concentration of protein in bacterial cells can be estimated to be
~135 mg/ml. In this session, we will explore how bacteria employ a suite of
molecular machines collectively known as chaperones to ensure that proteins
remain soluble and fold properly in such an extraordinarily crowded environment.
Specifically, we will discuss experiments that elucidate the mechanisms by which
aggregated or misfolded proteins can be reactivated and solubilized by the bacterial
Hsp100-family protein ClpB.
Paper for Discussion
1. Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, WeberBan EU, Dougan DA, Tsai F, Mogk A, Bukau B. Thermotolerance requires refolding of
aggregated proteins by substrate translocation through the central pore of ClpB. Cell
119:653-665.
Reviews
2. Doyle SM, Genest O, Wickner S. (2013) Protein rescue from aggregates by
powerful molecular chaperone machines. Nat. Rev. Mol. Cell Biol. 14:617-629.
3. Finka A, Mattoo R, Goloubinoff P. (2016) Experimental milestones in the
discovery of molecular chaperones as polypeptide unfolding enzymes. Annu. Rev.
Biochem. 85:715-742.