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RPA binds to ssDNA with high affinity, protecting it from nucleolytic degradation and preventing the formation of secondary structures that could impede DNA metabolism . The binding of RPA to ssDNA is essential for maintaining genome stability and facilitating the recruitment of other proteins involved in DNA transactions .
The RPA complex consists of several oligonucleotide/oligosaccharide binding (OB) domains, which are classified as either DNA-binding domains (DBDs) or protein-interaction domains. These domains enable RPA to interact with a variety of proteins and coordinate different DNA metabolic processes .
RPA interacts with numerous proteins to regulate DNA metabolism. One such protein is the RPA Interacting Protein (RPA-IP), which plays a critical role in modulating the function of RPA. RPA-IP can access the ssDNA buried under RPA by remodeling one or more domains without displacing RPA . This interaction is crucial for the proper functioning of RPA in DNA replication and repair.
The human recombinant form of RPA Interacting Protein is produced using recombinant DNA technology. This involves cloning the gene encoding RPA-IP into an expression vector, which is then introduced into a host cell (such as E. coli or yeast) to produce the protein. The recombinant protein is subsequently purified for research and therapeutic applications.
Recombinant RPA-IP is used in various studies to understand its role in DNA metabolism and its potential as a therapeutic target. By studying the recombinant form, researchers can gain insights into the molecular mechanisms underlying the interaction between RPA and RPA-IP and develop strategies to modulate this interaction for therapeutic purposes.