The DEAD-box helicase eIF4A1/2 acts as RNA chaperone during mitotic exit enabling chromatin decondensation

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
More Details
ISSN:20411723
DOI:10.1038/s41467-025-57592-1
Published in:Nature Communications
Language:English