Escherichia coli DnaK Allosterically Modulates ClpB between High- and Low-Peptide Affinity States.

Clicks: 244
ID: 67163
2018
Article Quality & Performance Metrics
Overall Quality Improving Quality
21.5 /100
Combines engagement data with AI-assessed academic quality
AI Quality Assessment
Not analyzed
Abstract
ClpB and DnaKJE provide protection to Escherichia coli cells during extreme environmental stress. Together, this co-chaperone system can resolve protein aggregates, restoring misfolded proteins to their native form and function in solubilizing damaged proteins for removal by the cell's proteolytic systems. DnaK is the component of the KJE system that directly interacts with ClpB. There are many hypotheses for how DnaK affects ClpB-catalyzed disaggregation, each with some experimental support. Here, we build on our recent work characterizing the molecular mechanism of ClpB-catalyzed polypeptide translocation by developing a stopped-flow FRET assay that allows us to detect ClpB's movement on model polypeptide substrates in the absence or presence of DnaK. We find that DnaK induces ClpB to dissociate from the polypeptide substrate. We propose that DnaK acts as a peptide release factor, binding ClpB and causing the ClpB conformation to change to a low-peptide affinity state. Such a role for DnaK would allow ClpB to rebind to another portion of an aggregate and continue nonprocessive translocation to disrupt the aggregate.
Reference Key
durie2018escherichiabiochemistry Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Durie, Clarissa L;Duran, Elizabeth C;Lucius, Aaron L;
Journal Biochemistry
Year 2018
DOI
10.1021/acs.biochem.8b00045
URL
Keywords
dietary survey mongolia adult male equivalent household consumption and expenditure intra-household distribution nutrient density nutrition surveillance

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.