Publication Date
1-12-2021
Journal
Nature Communications
DOI
10.1038/s41467-020-20553-x
PMID
33436616
PMCID
PMC7804408
PubMedCentral® Posted Date
1-12-2021
PubMedCentral® Full Text Version
Post-print
Published Open-Access
yes
Keywords
Binding Sites, Endopeptidase Clp, Escherichia coli, Escherichia coli Proteins, Gene Deletion, Genome, Bacterial, Magnetic Resonance Spectroscopy, Models, Biological, Models, Molecular, Molecular Chaperones, Mutagenesis, Peptides, Peptidylprolyl Isomerase, Phylogeny, Protein Binding, Protein Domains, Protein Interaction Mapping, Protein Multimerization, Proteolysis, Ribosomes, Substrate Specificity, Viral Proteins, Protein quality control, Chaperones
Abstract
A functional association is uncovered between the ribosome-associated trigger factor (TF) chaperone and the ClpXP degradation complex. Bioinformatic analyses demonstrate conservation of the close proximity of tig, the gene coding for TF, and genes coding for ClpXP, suggesting a functional interaction. The effect of TF on ClpXP-dependent degradation varies based on the nature of substrate. While degradation of some substrates are slowed down or are unaffected by TF, surprisingly, TF increases the degradation rate of a third class of substrates. These include λ phage replication protein λO, master regulator of stationary phase RpoS, and SsrA-tagged proteins. Globally, TF acts to enhance the degradation of about 2% of newly synthesized proteins. TF is found to interact through multiple sites with ClpX in a highly dynamic fashion to promote protein degradation. This chaperone-protease cooperation constitutes a unique and likely ancestral aspect of cellular protein homeostasis in which TF acts as an adaptor for ClpXP.
Comments
This article has been corrected. See Nat Commun. 2021 May 6;12:2753.
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