General Transcription Factor IIIC Polypeptide 6 (GTF3C6) is a crucial component of the transcription machinery in eukaryotic cells. It is a subunit of the larger General Transcription Factor IIIC (TFIIIC) complex, which is essential for the transcription of genes by RNA Polymerase III. This article delves into the structure, function, and significance of GTF3C6, particularly focusing on its human recombinant form.
GTF3C6 is a protein encoded by the GTF3C6 gene in humans. The protein consists of 213 amino acids and has a molecular weight of approximately 26 kDa . The recombinant form of GTF3C6 is often expressed in Escherichia coli and purified using conventional chromatography techniques . The protein typically includes a His tag at the N-terminus to facilitate purification and detection .
GTF3C6 plays a pivotal role in the assembly and function of the TFIIIC complex. TFIIIC is responsible for recognizing and binding to specific DNA sequences known as promoter regions, which are located upstream of genes transcribed by RNA Polymerase III. These genes include those encoding tRNAs, 5S rRNA, and other small RNAs essential for cellular function .
The TFIIIC complex consists of six subunits, and GTF3C6 is one of the smaller subunits. Despite its size, GTF3C6 is critical for the stability and activity of the entire complex. It interacts with other subunits to form a functional assembly that can recruit RNA Polymerase III to the promoter regions .
The proper functioning of GTF3C6 and the TFIIIC complex is vital for the transcription of genes involved in protein synthesis and other fundamental cellular processes. Dysregulation of TFIIIC components, including GTF3C6, can lead to various diseases and disorders. For instance, mutations or alterations in the GTF3C6 gene have been associated with certain types of cancer, such as pancreatic intraductal papillary-colloid carcinoma .
Recombinant GTF3C6 is widely used in research to study the structure and function of the TFIIIC complex. The recombinant protein is typically produced in E. coli and purified to high purity levels (>85%) for use in various biochemical assays . Researchers utilize recombinant GTF3C6 to investigate its interactions with other TFIIIC subunits, its role in transcription initiation, and its potential as a therapeutic target.