Abstract
The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. The nuclear pore complex assembly occurs on chromatin in the post-mitotic phase of the cell cycle. ELYS (MEL-28/AHCTF1) binds to the nucleosome, which is the basic chromatin unit, and promotes assembly of the complex around the chromosomes in cells. Here we show that the Arg-Arg-Lys (RRK) stretch of the C-terminal ELYS region plays an essential role in the nucleosome binding. The cryo-EM structure and the crosslinking mass spectrometry reveal that the ELYS C-terminal region directly binds to the acidic patch of the nucleosome. These results provide mechanistic insight into the ELYS-nucleosome interaction, which promotes the post-mitotic nuclear pore complex formation around chromosomes in cells.
Highlights
The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus
Reassembly of the nuclear envelope and nuclear pore complexes (NPCs) occurs at segregated chromosomes, and the functional nucleus is established in the daughter cells[10,11,13,14,15]
The Xenopus laevis ELYS protein is composed of 2408 amino acid residues, and its C-terminal region is reportedly involved in chromatin binding[18,22,23,24,25,26]
Summary
The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. ELYS (MEL-28/AHCTF1) binds to the nucleosome, which is the basic chromatin unit, and promotes assembly of the complex around the chromosomes in cells. The cryo-EM structure and the crosslinking mass spectrometry reveal that the ELYS C-terminal region directly binds to the acidic patch of the nucleosome These results provide mechanistic insight into the ELYS-nucleosome interaction, which promotes the post-mitotic nuclear pore complex formation around chromosomes in cells. In Caenorhabditis elegans, the knockdown of the ELYS homologue, MEL-28, induces an NPC assembly deficiency[19,20] These findings suggested that ELYS functions as a primer for the post-mitotic NPC reassembly on chromosomes[11,13,15,16,17,18,21]. The mechanistic details of the ELYS–nucleosome interaction have not been elucidated
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