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Cell Rep. 2015 Apr 14;11(2):321-33. doi: 10.1016/j.celrep.2015.03.018. Epub 2015 Apr 2.

Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.

Author information

1
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.
2
Departments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USA.
3
Department of Mathematics and Computer Science, Clarkson University, Potsdam, NY 13699, USA.
4
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
5
Departments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USA. Electronic address: gierasch@biochem.umass.edu.
6
Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: epowers@scripps.edu.

Abstract

The folding fate of a protein in vivo is determined by the interplay between a protein's folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual components of the E. coli proteostasis network have been studied extensively, but much less is known about how they function as a system. We used an integrated experimental and computational approach to quantitatively analyze the folding outcomes (native folding versus aggregation versus degradation) of three test proteins biosynthesized in E. coli under a variety of conditions. Overexpression of the entire proteostasis network benefited all three test proteins, but the effect of upregulating individual chaperones or the major degradation enzyme, Lon, varied for proteins with different biophysical properties. In sum, the impact of the E. coli proteostasis network is a consequence of concerted action by the Hsp70 system (DnaK/DnaJ/GrpE), the Hsp60 system (GroEL/GroES), and Lon.

PMID:
25843722
PMCID:
PMC4401642
DOI:
10.1016/j.celrep.2015.03.018
[Indexed for MEDLINE]
Free PMC Article

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