Early steps of E. coli DMSO reductase maturation and the interplay of general chaperones Trigger Factor and DnaK with the specific chaperone DmsD.
Date
2013-02-11
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Abstract
Bacterial oxidoreductases play a key role in anaerobic respiration and represent a group of enzymes with complex maturation pathways. A group of specific chaperones, or redox enzyme maturation proteins (REMP), have been shown to interact tightly with the amino terminal signal peptide of oxidoreductase subunits. DmsD, the REMP associated with the oxidoreductase dimethyl sulfoxide (DMSO) reductase, has been putatively shown to interact with two general chaperones, DnaK and Trigger Factor (TF). Here, we begin to characterize the protein interactions between DnaK and TF and the DMSO reductase maturation system. DmsD was found not to associate with the ribosome for early access to its peptide substrate E. coli deficient in DnaK or TF grew more slowly when forced to respire DMSO, linking them to DMSO reductase maturation. While interactions could not be found between DnaK or TF and DmsD, both chaperones interacted with the signal peptide of DMSO reductase.
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Biochemistry
Citation
Leach, T. G. (2013). Early steps of E. coli DMSO reductase maturation and the interplay of general chaperones Trigger Factor and DnaK with the specific chaperone DmsD. (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/25772