Nucleolin is composed of several structural domains that enable it to interact with different proteins and RNA sequences. It is an abundant protein in the nucleolus, accounting for up to 10% of the total nucleolar protein in some cells . The protein is approximately 100-110 kDa in size, although the predicted molecular mass based on its amino acid sequence is around 77 kDa .
The primary functions of nucleolin include:
Nucleolin is essential for the growth and proliferation of eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles, indicating its role in the early stages of ribosome assembly . Additionally, nucleolin has been implicated in the regulation of transcription by RNA polymerase I and II, angiogenesis, and cellular responses to various stimuli .
Nucleolin has been studied for its potential role in various diseases. For instance, it acts as a low-affinity receptor for certain growth factors and can inhibit HIV infection by binding to the virus . Moreover, nucleolin at the cell surface serves as a receptor for the respiratory syncytial virus (RSV) fusion protein, highlighting its importance in viral infections .
Recombinant nucleolin is produced using genetic engineering techniques to express the human nucleolin protein in a host organism, such as bacteria or yeast. This allows for the large-scale production and purification of nucleolin for research and therapeutic purposes. Recombinant nucleolin retains the functional properties of the native protein and is used in various studies to understand its role in cellular processes and disease mechanisms.