TAF15 is a member of the FET (FUS, EWS, TAF15) family of proteins, which are structurally similar and multifunctional . These proteins were initially discovered due to their involvement in fusion oncogenes in human sarcomas and leukemias . TAF15 contains RNA recognition motifs (RRMs) and glycine-rich regions, which enable it to bind RNA and DNA .
The primary function of TAF15 is to facilitate the assembly of the transcription complex by interacting with other transcription factors and coactivators . It plays a crucial role in the regulation of gene expression by binding to the core promoter region of genes and positioning RNA polymerase II correctly . Additionally, TAF15 is involved in various cellular processes, including RNA splicing, transport, and stability .
Recombinant TAF15 is a form of the protein that is produced using recombinant DNA technology. This involves inserting the TAF15 gene into an expression vector, which is then introduced into a host cell (such as E. coli) to produce the protein . The recombinant protein can be purified and used for various research applications, including studying its function, interactions, and role in diseases .
The recombinant TAF15 protein typically includes a His-tag at the N-terminus to facilitate purification . It corresponds to the amino acids 148-406 of the human TAF15 protein .
TAF15 has been implicated in several diseases, particularly cancers. Translocations involving the TAF15 gene and other genes, such as the nuclear receptor CSMF, result in fusion proteins that are associated with a subset of extraskeletal myxoid chondrosarcomas . These fusion proteins can disrupt normal cellular functions and contribute to tumorigenesis .
Furthermore, TAF15 is involved in the regulation of transcription by RNA polymerase II, which is a critical process in maintaining cellular homeostasis and responding to various signals . Dysregulation of this process can lead to various diseases, including cancer .