Elongator acetyltransferase complex subunit 6 (Elp6)

Elongator acetyltransferase complex subunit 6 (Elp6) is one of six subunits of the Elongator complex, a multiprotein complex conserved from yeast to humans. Elp6 assembles with Elp4 and Elp5 to form a heterohexameric (ring-like) accessory subcomplex (Elp4–6), which is indispensable for the structural integrity and function of the full Elongator complex. Structurally, Elp6 and its partners (Elp4, Elp5) share a RecA-like fold but lack ATPase activity. The Elongator complex is involved in transcriptional elongation by RNA polymerase II, tRNA modification (notably, modification of wobble uridines), and other processes like histone acetylation and cytoskeleton regulation. While Elp6 does not possess catalytic activity, its structural role is critical in complex assembly and function, especially in substrate binding and recognition required for proper tRNA modification and possibly histone H3 acetylation. Mutations in the Elongator complex are linked to various neurodevelopmental diseases, but Elp6 itself is not typically mutated in these disorders. There is no evidence that Elongator acetyltransferase complex subunit 6 is considered a stand-alone therapeutic target, nor is it the site of direct drug action or patient biomarker utility.

Other names

ELP6Elongator complex protein 6

Not applicable (no known drugs target Elp6 directly)