SKP E. Coli
Description
Product Specs
Product Science Overview
Chaperone proteins play a crucial role in assisting the proper folding and assembly of other proteins within the cell. One such chaperone protein is SKP (Seventeen Kilodalton Protein), which is particularly significant in the context of Escherichia coli (E. coli). This article delves into the background, function, and importance of SKP in recombinant protein production in E. coli.
SKP is a periplasmic chaperone protein in E. coli, with a molecular weight of approximately 18 kDa . It is involved in the folding and assembly of outer membrane proteins (OMPs), ensuring they achieve their correct conformation and maintain solubility . SKP operates in the periplasmic space, the area between the inner cytoplasmic membrane and the outer membrane of the bacterial cell.
The primary function of SKP is to prevent the aggregation of newly synthesized OMPs by binding to them and facilitating their proper folding . This is particularly important because misfolded proteins can form insoluble aggregates that are detrimental to cell viability and function. By assisting in the correct folding of OMPs, SKP helps maintain the integrity and functionality of the bacterial outer membrane.
In the field of biotechnology, E. coli is a widely used host for the production of recombinant proteins due to its rapid growth and well-characterized genetics. However, the overproduction of recombinant proteins often leads to misfolding and aggregation, resulting in low yields of functional protein . To address this issue, co-expression of chaperone proteins like SKP has been employed to enhance the solubility and functionality of recombinant proteins .
Studies have shown that the co-expression of SKP with other chaperones, such as FkpA, can significantly improve the solubility and yield of recombinant proteins . For instance, the co-expression of SKP and FkpA has been demonstrated to enhance the solubility and cell viability during the production of single-chain variable fragment (scFv) antibodies in E. coli . This synergistic effect is attributed to the combined chaperone activities that assist in the proper folding and stabilization of the target proteins.
SKP functions by forming a protective complex around the unfolded or partially folded OMPs, preventing their aggregation . This complex is then delivered to the outer membrane, where the OMPs can be inserted and achieve their native conformation. The exact mechanism involves the recognition of hydrophobic regions of the OMPs by SKP, which shields these regions from the aqueous environment of the periplasm .
