Elongator acetyltransferase complex subunit 3 (ELP3)

Elongator acetyltransferase complex subunit 3 (ELP3) is the catalytic core subunit of the Elongator complex, which is highly conserved in eukaryotes and present across all domains of life. Its primary function is to catalyze post-transcriptional modifications of tRNAs, specifically acetylating uridine at the wobble position (U34), a process essential for accurate translation and proteome maintenance. ELP3 houses two main domains: a radical S-adenosyl methionine (rSAM) domain and a lysine acetyltransferase (KAT) domain, enabling it to perform unique tRNA and histone modifications. Beyond translation, ELP3 has been shown to participate in histone acetylation, transcriptional elongation, neuronal development, DNA repair, and other cellular processes. Mutations or deficiency of ELP3 are associated with a wide range of human diseases, particularly neurodevelopmental and neurodegenerative disorders, as well as cancer. Its essential cellular functions and disease associations make it a potential therapeutic and research target, although no approved drugs currently act directly on ELP3.

Other names

Elongator complex protein 3ELP3hELP3FLJ10422KAT9tRNA uridine(34) acetyltransferaseElongation protein 3 homologProtein lysine acetyltransferase ELP3

Drugs or inhibitors would typically act by inhibiting the acetyltransferase activity (blocking the KAT or rSAM domain activity, thus preventing tRNA or histone acetylation). Potential mechanism: substrate competition, allosteric inhibition, or direct blockade of cofactor (acetyl-CoA or SAM) binding sites.