Dimerization of elongator protein 1 is essential for Elongator complex assembly

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Abstract
Significance: Elongator is a highly conserved multiprotein complex composed of six subunits elongator protein 1 (Elp1 to -6). Elongator has been associated with various cellular activities and has attracted clinical attention because of its role in certain neurodegenerative diseases. To understand the mechanism of Elongator assembly, we identified the highly conserved dimerization domain in both human and yeast Elp1 subunits and solved the crystal structures of the dimerization domains. This study is a mechanistic analysis of Elp1 dimerization, which plays an essential role in the integrity of functional Elongator and suggests that the pathological mechanisms underlying the onset and progression of Elp1 mutation-related diseases may result from impaired Elongator activities.

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