Recombinant Synechococcus sp. Deoxyribodipyrimidine photo-lyase (phr)

Amino acids 2-484 form the expressed segment for recombinant Synechococcus sp. phr. The calculated molecular weight for this phr protein is 74.3 kDa. This protein is generated in a e.coli-based system. The N-terminal 10xHis-SUMO tag and C-terminal Myc tag was smoothly integrated into the coding gene of phr, which enables a simple process of detecting and purifying the phr recombinant protein in the following steps.

The Synechococcus sp. deoxyribodipyrimidine photo-lyase (Phr) is an enzyme that plays a critical role in the repair of DNA damage caused by ultraviolet (UV) radiation. Upon absorption of light in the visible or near-UV range, Phr undergoes a conformational change and becomes activated. The activated Phr can then bind to damaged DNA containing CPDs or 6-4 photoproducts. Through a process known as photoreactivation, the Phr enzyme utilizes energy from light to break the covalent bonds within the DNA lesions, restoring the original structure of the DNA strand. The function of Phr is particularly important for organisms like Synechococcus sp. that are exposed to natural sunlight, as it provides a mechanism to repair UV-induced DNA damage and maintain genomic integrity. Studying photo-lyases, including Synechococcus sp. Phr contributes to the understanding of DNA repair mechanisms and has implications for various biotechnological applications, such as the development of photoreactivation-based technologies for DNA repair in diverse organisms.