Ribosomal Protein L30 (RPL30) is a crucial component of the large 60S subunit of eukaryotic ribosomes. It belongs to the L30E family of ribosomal proteins and plays a significant role in the synthesis of proteins within the cell. This article delves into the structure, function, and significance of RPL30, with a focus on its human recombinant form.
RPL30 is encoded by the RPL30 gene, which is located in the cytoplasm. The gene is co-transcribed with the U72 small nucleolar RNA gene, located in its fourth intron . The protein itself is a part of the large ribosomal subunit and is involved in forming a bridge between the large and small subunits of the ribosome .
RPL30 is essential for the proper functioning of the ribosome. It binds to kink-turn motifs in the 28S ribosomal RNA, L30 pre-mRNA, and mature L30 mRNA . Additionally, RPL30 has a noncanonical function as a component of the UGA recoding machinery, which incorporates selenocysteine into selenoproteins during translation . This function is crucial for the synthesis of selenoproteins, which are important for various cellular processes.
One of the unique aspects of RPL30 is its interaction with the Sec Insertion Sequence (SECIS) element in the 3’ untranslated region (UTR) of mammalian selenoprotein mRNAs . The SECIS element is essential for the incorporation of selenocysteine into proteins. RPL30 binds to a putative kink-turn motif in the SECIS element, competing with SECIS-binding protein 2 (SBP2) for binding . This competitive binding is crucial for the regulation of selenoprotein synthesis.
Recombinant human RPL30 protein is typically produced in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant form is often fused to a His-tag at the N-terminus to facilitate purification and detection . This recombinant protein is used in various research applications to study the function and interactions of RPL30.