The Elp2 subunit is essential for elongator complex assembly and functional regulation
| Autor: | Jiafu Long, Zhijie Lin, Yuequan Shen, Chunming Dong, Dan Li, Zhiping Xie, Zheng Wang, Wentao Diao, Xinlei Chu, Hao Zhou |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Multiprotein complex Saccharomyces cerevisiae Proteins Immunoprecipitation Protein subunit Immunoblotting Molecular Sequence Data Plasma protein binding Biology ELP3 Protein structure Microtubule Structural Biology Humans Amino Acid Sequence Histone H3 acetylation Molecular Biology Genetics Cell biology Protein Structure Tertiary HEK293 Cells Multiprotein Complexes Microtubule Proteins Microtubule-Associated Proteins Protein Binding |
| Zdroj: | Structure (London, England : 1993). 23(6) |
| ISSN: | 1878-4186 |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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