The NOP16 gene is located on chromosome 5 in humans. It encodes a protein that is primarily localized in the nucleolus, a substructure within the nucleus responsible for ribosome production. The human recombinant NOP16 protein is typically expressed in E. coli and is a single, non-glycosylated polypeptide chain containing 201 amino acids, with a molecular weight of approximately 23.6 kDa . It is often fused to a His-tag at the N-terminus to facilitate purification.
NOP16 expression is regulated by estrogens and the MYC protein . This regulation is significant because MYC is a well-known oncogene, and its overexpression is associated with various cancers, including breast cancer. High levels of NOP16 have been correlated with poor clinical outcomes in breast cancer patients, making it a potential biomarker for prognosis .
NOP16 plays a crucial role in ribosome biogenesis, which is essential for protein synthesis and cell growth. It is involved in the maturation of the 60S ribosomal subunit, a component of the ribosome. The protein’s expression is induced by estrogens and MYC, linking it to cell proliferation and cancer progression .
The clinical significance of NOP16 lies in its potential as a biomarker for cancer prognosis. Studies have shown that high expression levels of NOP16 are associated with aggressive tumor characteristics and poor survival rates in breast cancer patients . This makes NOP16 a valuable target for cancer research and potential therapeutic interventions.
Recombinant NOP16 is produced using recombinant DNA technology, which involves inserting the NOP16 gene into a suitable expression system, such as E. coli. The recombinant protein is then purified using various techniques, including affinity chromatography, which exploits the His-tag fused to the protein . This recombinant form is used in research to study the protein’s function, structure, and role in disease.