THAP7 Human

THAP7 is a chromatin-associated protein that binds to histone tails and represses transcription by recruiting histone deacetylase 3 (HDAC3) and nuclear hormone receptor corepressors . The human recombinant form of THAP7 is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 332 amino acids, with a molecular mass of approximately 36.8 kDa . It includes a 23 amino acid His-tag at the N-terminus, which facilitates its purification through chromatographic techniques .

THAP7 is involved in the repression of transcription by interacting with other proteins and chromatin components. It associates with template-activating factor-Iβ (TAF-Iβ), also known as PHAPII, SET, and I2PP2A, which is a component of the inhibitor of acetyltransferases (INHAT) complex . This complex masks histone acetylation and blocks histone acetyltransferase (HAT)-dependent transcription, thereby maintaining histones in a hypoacetylated, repressed state .

THAP7 also interacts with histone H3 and histone H4, inhibiting their acetylation . This interaction is crucial for its role in transcriptional repression, as acetylation of histones is generally associated with transcriptional activation. By preventing histone acetylation, THAP7 helps to maintain a repressed chromatin state, thereby regulating gene expression.

The regulation of chromatin structure and histone modifications is critical for the control of gene expression. THAP7, through its interactions with histones and other chromatin-associated proteins, plays a vital role in this process. Its ability to recruit corepressors and inhibit histone acetylation highlights its importance in maintaining the balance between transcriptional activation and repression.