Journal
STRUCTURE
Volume 21, Issue 4, Pages 572-580Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.02.006
Keywords
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Funding
- National Institutes of Health [GM077537]
- Pew Scholar Award
- Croatian Science Foundation
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In metazoa, the nuclear envelope (NE), together with the embedded nuclear pore complexes (NPCs), breaks down and reassembles during cell division. It is suggested that ELYS, a nucleoporin, binds to chromatin in an initial step of postmitotic NPC assembly and subsequently recruits the essential Y-subcomplex, the major scaffolding unit of the NPC. Here, we show that ELYS contains three domains: an N-terminal beta-propeller domain, a central a-helical domain, and a C-terminal disordered region. While the disordered region is responsible for the interactions with chromatin, the two preceding domains synergistically mediate tethering to the NPC. We present the crystal structure of the seven-bladed beta-propeller domain at 1.9 angstrom resolution. Analysis of the beta-propeller surface reveals the regions that are required for NPC anchorage. We discuss the possible roles of ELYS in the context of the NPC scaffold architecture.
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