RPLP0 is a neutral phosphoprotein that belongs to the L10P family of ribosomal proteins . It is the functional equivalent of the bacterial L10 protein and is a part of the ribosomal stalk, which also includes the acidic phosphoproteins P1 and P2. The C-terminal end of RPLP0 is nearly identical to the C-terminal ends of P1 and P2, which allows it to form a complex with these proteins .
The primary function of RPLP0 is to anchor the P1 and P2 proteins to the ribosome, forming a pentameric complex (P0-(P1-P2)2). This complex is crucial for the ribosome’s interaction with elongation factors during the translation process, thereby playing a vital role in protein synthesis.
Recombinant RPLP0 can be produced in various expression systems, including Escherichia coli and Sf9 insect cells . The protein is often expressed with tags such as His-T7 or His to facilitate purification. For instance, RPLP0 expressed in E. coli is typically purified using chromatographic techniques and has a purity greater than 90% . In contrast, RPLP0 produced in Sf9 insect cells is glycosylated and has a molecular mass of approximately 35,096 Daltons .
Recombinant RPLP0 has several applications in biomedical research. It is used in studies related to protein synthesis, ribosome structure, and function. Additionally, it is employed in various assays, including ELISA and Western blotting, to detect auto-antibodies in diseases such as systemic lupus erythematosus (SLE) .