Recombinant E.coli degP protein

DegP, also known as HtrA (High-temperature requirement A), is a bifunctional protease and chaperone protein originally identified in *Escherichia coli*. It plays a critical role in bacterial stress responses by degrading misfolded proteins or assisting in their refolding under conditions such as heat shock, oxidative stress, or envelope protein dysregulation. Structurally, DegP consists of a trypsin-like protease domain and two PDZ domains that regulate substrate recognition and oligomerization. Its activity is tightly controlled through temperature-dependent conformational changes, transitioning from chaperone-like hexamers at lower temperatures to proteolytically active 12- or 24-mers under stress.

Recombinant DegP (rDegP) is engineered for overexpression and purification in heterologous systems like *E. coli*. This allows detailed study of its dual enzymatic functions, substrate specificity, and structural dynamics. Research highlights its role in bacterial pathogenesis, as DegP homologs in pathogens (e.g., *Salmonella*, *Helicobacter pylori*) contribute to virulence by degrading host defense proteins or maintaining envelope integrity. Biotechnological applications exploit rDegP’s ability to degrade aggregation-prone proteins during recombinant protein production, enhancing yield and purity. Additionally, its stress-responsive properties inspire synthetic biology designs for protein quality control systems. However, uncontrolled proteolysis by DegP can complicate bioprocessing, driving studies on regulatory mechanisms like allosteric PDZ domain interactions. Current efforts also target DegP as a therapeutic candidate, with inhibitors under investigation to disrupt bacterial survival mechanisms. Overall, rDegP serves as a versatile tool for probing bacterial stress adaptation while offering industrial and medical potential.