KAT2A Human

K (Lysine) Acetyltransferase 2A, also known as KAT2A or GCN5, is a member of the histone acetyltransferase (HAT) family. This enzyme plays a crucial role in the regulation of gene expression by modifying chromatin structure through the acetylation of lysine residues on histone proteins. The human recombinant form of KAT2A is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism, such as E. coli, to facilitate its study and use in various applications.

KAT2A is a multi-functional enzyme that can act as an acetyltransferase, glutaryltransferase, succinyltransferase, or malonyltransferase, depending on the context . It primarily functions as a transcriptional activator by acetylating lysine residues on histone proteins, which leads to a more relaxed chromatin structure and increased gene expression . Additionally, KAT2A has been shown to acetylate non-histone proteins, such as the cell-division cycle protein 6 (CDC6), CCAAT/enhancer-binding protein beta (C/EBPβ), and polo-like kinase 4 (PLK4), thereby regulating various cellular processes .

The acetylation of histone proteins by KAT2A is a key epigenetic modification that plays a vital role in the regulation of gene expression. This modification is associated with transcriptional activation and is essential for various cellular processes, including cell cycle progression, DNA repair, and differentiation . KAT2A also functions as a repressor of the NF-kappa-B signaling pathway by promoting the ubiquitination of the NF-kappa-B subunit RELA in a HAT-independent manner .

The human recombinant form of KAT2A is produced in E. coli as a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 51.1 kDa . This recombinant protein is fused to a 20 amino acid His-tag at the N-terminus, which facilitates its purification using chromatographic techniques . The availability of human recombinant KAT2A allows for detailed studies of its structure, function, and interactions with other proteins, as well as its use in various biochemical assays and drug discovery efforts.

Mutations and dysregulation of KAT2A have been associated with several diseases, including spinocerebellar ataxia 7 and Desbuquois dysplasia . Understanding the role of KAT2A in these diseases can provide insights into their underlying mechanisms and potentially lead to the development of targeted therapies.