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PDBsum entry 4xfv
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References listed in PDB file
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Key reference
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Title
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The elp2 subunit is essential for elongator complex assembly and functional regulation.
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Authors
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C.Dong,
Z.Lin,
W.Diao,
D.Li,
X.Chu,
Z.Wang,
H.Zhou,
Z.Xie,
Y.Shen,
J.Long.
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Ref.
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Structure, 2015,
23,
1078-1086.
[DOI no: ]
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PubMed id
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Abstract
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Elongator is a highly conserved multiprotein complex composed of six subunits
(Elp1-6). Elongator has been associated with various cellular activities and has
attracted clinical attention because of its role in certain neurodegenerative
diseases. Here, we present the crystal structure of the Elp2 subunit revealing
two seven-bladed WD40 β propellers, and show by structure-guided mutational
analyses that the WD40 fold integrity of Elp2 is necessary for its binding to
Elp1 and Elp3 subunits in multiple species. The detailed biochemical experiments
indicate that Elp2 binds microtubules through its conserved alkaline residues
in vitro and in vivo. We find that both the mutually independent Elp2-mediated
Elongator assembly and the cytoskeleton association are important for yeast
viability. In addition, mutation of Elp2 greatly affects the histone H3
acetylation activity of Elongator in vivo. Our results indicate that Elp2 is a
necessary component for functional Elongator and acts as a hub in the formation
of various complexes.
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