TCEA2 is characterized by its ability to stimulate RNA polymerase II to overcome transcriptional arrest. This is achieved through its interaction with the polymerase, promoting the cleavage of the nascent RNA and allowing the polymerase to resume transcription. The protein contains several conserved domains that are essential for its function, including the central domain responsible for RNA cleavage activity.
The role of TCEA2 in transcription elongation is vital for the proper expression of genes. It ensures that RNA polymerase II can efficiently transcribe genes, even in the presence of obstacles such as DNA damage or tightly packed chromatin. This function is particularly important in rapidly dividing cells and in response to cellular stress, where efficient gene expression is crucial.
Recombinant human TCEA2 is produced using various expression systems, with Escherichia coli being one of the most common hosts. The recombinant protein is typically fused with tags, such as His-tags, to facilitate purification. The production of recombinant TCEA2 allows for detailed studies of its structure and function, as well as its interactions with other proteins involved in transcription.
Recombinant TCEA2 is widely used in biochemical and structural studies to understand the mechanisms of transcription elongation. It is also employed in assays to screen for potential inhibitors of transcription, which could be valuable in developing therapeutic strategies for diseases associated with dysregulated gene expression.