| Literature DB >> 25960406 |
Chunming Dong1, Zhijie Lin1, Wentao Diao1, Dan Li2, Xinlei Chu1, Zheng Wang1, Hao Zhou1, Zhiping Xie2, Yuequan Shen3, Jiafu Long4.
Abstract
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.Entities:
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Year: 2015 PMID： 25960406 DOI： 10.1016/j.str.2015.03.018
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006