GTF2A1 Human

TFIIA is composed of multiple subunits, with the GTF2A1 gene encoding the alpha and beta subunits of this factor . These subunits form a complex that interacts with the TATA-binding protein (TBP) and stabilizes its binding to the DNA promoter regions. This stabilization is essential for the formation of the transcription pre-initiation complex, which is necessary for the accurate initiation of transcription .

The primary function of TFIIA is to facilitate the binding of TBP to the TATA box, a DNA sequence found in the promoter region of many genes. By stabilizing this interaction, TFIIA helps to recruit other general transcription factors and RNA polymerase II to the promoter, thereby enabling the transcription of genes into mRNA .

Recombinant human TFIIA is produced using recombinant DNA technology, where the GTF2A1 gene is cloned and expressed in a suitable host, such as Escherichia coli. This allows for the production of large quantities of the protein for research and therapeutic purposes . The recombinant protein retains the functional properties of the native protein, making it a valuable tool for studying transcription mechanisms and for potential therapeutic applications .

TFIIA is not only important for general transcription but also plays a role in specific biological processes. For instance, it has been implicated in testis biology, where it may function as a testis-specific transcription factor . Additionally, mutations or dysregulation of TFIIA components can lead to various diseases, including mitochondrial DNA depletion syndrome and certain forms of dystonia .

The availability of recombinant human TFIIA has facilitated numerous studies aimed at understanding the detailed mechanisms of transcription initiation. It is also used in various assays to study protein-DNA interactions, transcription factor binding, and the effects of mutations on transcriptional activity .