Serine/arginine-rich splicing factor 1 (SRSF1), also known as ASF/SF2, is a crucial protein involved in the regulation of pre-mRNA splicing. This protein is encoded by the SRSF1 gene located on chromosome 17 in humans . SRSF1 is a member of the SR protein family, characterized by the presence of serine/arginine-rich domains that play a significant role in RNA splicing and other post-transcriptional processes .
The SRSF1 gene spans approximately 7.4 kb and consists of multiple exons that encode a protein of about 33 kDa . The protein contains two RNA recognition motifs (RRMs) at the N-terminus and a serine/arginine-rich domain at the C-terminus . These domains are essential for its interaction with RNA and other splicing factors, facilitating the formation of the spliceosome complex .
SRSF1 is involved in both constitutive and alternative splicing of pre-mRNA . It binds to exonic splicing enhancers (ESEs) and recruits other components of the spliceosome to the splice sites . This process ensures the accurate removal of introns and the joining of exons, which is crucial for the generation of mature mRNA .
In addition to its role in splicing, SRSF1 is also involved in mRNA nuclear export, translation, and stability . It interacts with various proteins and RNA sequences to regulate these processes, thereby influencing gene expression at multiple levels .
SRSF1 plays a vital role in cellular homeostasis and development . It is essential for the proper functioning of various biological pathways, including those involved in cell cycle regulation, apoptosis, and differentiation . Dysregulation of SRSF1 has been implicated in several diseases, including cancer, where it can act as an oncogene by promoting the expression of splice variants that drive tumorigenesis .
Human recombinant SRSF1 is produced using recombinant DNA technology, which involves the insertion of the SRSF1 gene into an expression vector and its subsequent expression in a host organism, such as bacteria or yeast . This allows for the large-scale production of the protein for research and therapeutic purposes .