Recombinant E. coli DsbE protein

**Background of DRG1 Recombinant Protein**

DRG1 (Developmentally Regulated GTP-binding Protein 1), also termed *RGD1* or *DIR1*, is a highly conserved GTP-binding protein belonging to the **DRG subfamily** within the **TRAFAC class of GTPases**. First identified in studies on developmental regulation, DRG1 is ubiquitously expressed across eukaryotes and plays roles in cell growth, differentiation, and stress responses. Structurally, it contains a canonical GTP-binding domain and a unique C-terminal domain implicated in protein-protein interactions.

Functionally, DRG1 is linked to **translational regulation** and **RNA metabolism**, though its precise molecular mechanisms remain under investigation. It interacts with ribonucleoprotein complexes and modulates cellular processes such as mRNA stability and translation efficiency. Emerging evidence highlights its involvement in **tumor suppression** or **oncogenesis**, depending on cellular context. For instance, DRG1 is downregulated in certain cancers (e.g., colorectal, breast), correlating with poor prognosis, while overexpression in other malignancies may drive metastasis.

Recombinant DRG1 protein is produced via heterologous expression systems (e.g., *E. coli*, mammalian cells*) for *in vitro* studies. Its purified form enables exploration of enzymatic activity, GTPase kinetics, and interaction partners. Researchers utilize DRG1 recombinant protein to dissect its role in **stress adaptation** (e.g., hypoxia, nutrient deprivation) and **therapeutic targeting**, particularly in cancer. Additionally, structural studies using recombinant DRG1 aim to resolve its conformational dynamics during GTP hydrolysis, offering insights into regulatory mechanisms.

In summary, DRG1 represents a multifaceted GTPase with implications in development, disease, and cellular homeostasis, making its recombinant form a vital tool for functional and biomedical research.

DsbE, a periplasmic oxidoreductase from *Escherichia coli*, plays a critical role in catalyzing disulfide bond formation during protein folding. As a member of the thioredoxin superfamily, it contains a conserved CXXC active-site motif (Cys-Gly-Cys-Lys in DsbE) responsible for its redox activity. Unlike its homolog DsbA, which primarily oxidizes cysteine residues in nascent polypeptides, DsbE exhibits unique substrate specificity and functional versatility, often acting as a disulfide isomerase to resolve misfolded bonds in periplasmic or secreted proteins.

Recombinant DsbE is engineered for biotechnological applications, particularly in enhancing the production of correctly folded proteins in heterologous expression systems. In *E. coli*, overexpression of DsbE improves the yield of functional disulfide-rich proteins, such as antibodies or enzymes, by optimizing oxidative folding. Its role extends beyond prokaryotes; modified variants or fusion constructs of DsbE are explored in eukaryotic systems to address challenges in recombinant protein production, including aggregation and misfolding.

Structurally, DsbE’s compact α-helical domain and flexible N-terminal region enable interactions with diverse substrates. Studies highlight its redox potential (−140 mV), which is less oxidizing than DsbA, allowing fine-tuned regulation of disulfide bond formation. Research also links DsbE to bacterial virulence, as it assists in folding pathogenicity factors in pathogenic strains.

Overall, recombinant DsbE serves as a vital tool in synthetic biology and industrial protein production, bridging gaps in understanding oxidative folding mechanisms while offering solutions for manufacturing complex therapeutic proteins. Its engineering and functional analysis continue to drive innovations in biopharmaceutical development.