A Conserved Acidic Amino Acid Mediates the Interaction between Modulators and Co-Chaperones in Enterobacteria

Hsp40-like co-chaperones are ubiquitous enzymes that stimulate the protein refolding activity of Hsp70 family chaperones. They are widespread in prokaryotic and eukaryotic systems. In bacteria, the best characterized co-chaperone is the Escherichia coli DnaJ protein. Many γ-proteobacteria encode a functional homologue of DnaJ, known as CbpA, which is expressed in response to starvation and environmental stress. The activity of CbpA is regulated by the “modulator” protein CbpM. Here, we have used a combination of genetics and biochemistry to identify the co-chaperone contact determinant of CbpM. We show that the nature of the interaction is conserved in enterobacteria.

Graphical AbstractFigure optionsDownload full-size imageDownload high-quality image (91 K)Download as PowerPoint slideResearch Highlights► Characterization of the interaction between modulator and co-chaperone proteins. ► Investigation of interspecies modulator–co-chaperone interactions. ► Reversal of co-chaperone aggregation by a modulator protein.