NAA30 Human

NAA30 catalyzes the acetylation of the N-terminal methionine residues of peptides that begin with specific sequences, such as Met-Leu-Ala and Met-Leu-Gly . This process, known as N-terminal acetylation, is a common and functionally significant modification in eukaryotic proteins. It plays a crucial role in various cellular processes, including protein stability, localization, and interaction .

The NatC complex, which includes NAA30, is involved in co-translational acetylation, meaning it acetylates proteins as they are being synthesized by ribosomes . This complex is essential for the proper localization and function of certain proteins, such as ARL8B, which is necessary for lysosomal function .

The NAA30 gene is located on chromosome 14q22.3 and consists of four exons . The protein encoded by this gene contains 362 amino acids and includes a bipartite nuclear localization signal and an acetyl coenzyme A-binding domain . There are also truncated variants of NAA30 that lack certain regions of the full-length protein, affecting its localization and function .

Mutations or dysregulation of the NAA30 gene have been associated with various diseases, including Ogden Syndrome and uterine corpus endometrial carcinoma . The protein’s role in N-terminal acetylation makes it a critical player in maintaining cellular homeostasis and function, and its dysfunction can lead to significant pathological conditions .

Research on NAA30 and the NatC complex continues to uncover its broader implications in cellular biology and disease. The recombinant form of NAA30 is used in various biochemical assays to study its enzymatic activity and interactions with other proteins. Understanding the detailed mechanisms of NAA30 can provide insights into potential therapeutic targets for diseases associated with its dysfunction .