Bibliographic Details
Title: |
The DEAD-box helicase eIF4A1/2 acts as RNA chaperone during mitotic exit enabling chromatin decondensation |
Authors: |
Ramona Jühlen, Sabine C. Wiesmann, Anja Scheufen, Thilo Stausberg, Isabel Braun, Chantal Strobel, Carmen Llera-Brandt, Sabrina Rappold, Rabia Suluyayla, Marianna Tatarek-Nossol, Birgitt Lennartz, Hongqi Lue, Maximilian W. G. Schneider, Juan-Felipe Perez-Correa, Daniel Moreno-Andrés, Wolfram Antonin |
Source: |
Nature Communications, Vol 16, Iss 1, Pp 1-17 (2025) |
Publisher Information: |
Nature Portfolio, 2025. |
Publication Year: |
2025 |
Collection: |
LCC:Science |
Subject Terms: |
Science |
More Details: |
Abstract During mitosis, chromosomes condense and decondense to segregate faithfully and undamaged. The exact molecular mechanisms are not well understood. We identify the DEAD-box helicase eIF4A1/2 as a critical factor in this process. In a cell-free condensation assay eIF4A1/2 is crucial for this process, relying on its RNA-binding ability but not its ATPase activity. Reducing eIF4A1/2 levels in cells consistently slows down chromatin decondensation during nuclear reformation. Conversely, increasing eIF4A1/2 concentration on mitotic chromosomes accelerates their decondensation. The absence of eIF4A1/2 affects the perichromatin layer, which surrounds the chromosomes during mitosis and consists of RNA and mainly nucleolar proteins. In vitro, eIF4A1/2 acts as an RNA chaperone, dissociating biomolecular condensates of RNA and perichromatin proteins. During mitosis, the chaperone activity of eIF4A1/2 is required to regulate the composition and fluidity of the perichromatin layer, which is crucial for the dynamic reorganization of chromatin as cells exit mitosis. |
Document Type: |
article |
File Description: |
electronic resource |
Language: |
English |
ISSN: |
2041-1723 |
Relation: |
https://doaj.org/toc/2041-1723 |
DOI: |
10.1038/s41467-025-57592-1 |
Access URL: |
https://doaj.org/article/d1ffe3b090e14481a52ee1e3686a0fbe |
Accession Number: |
edsdoj.1ffe3b090e14481a52ee1e3686a0fbe |
Database: |
Directory of Open Access Journals |