Modulation of RNA Condensation by the DEAD-Box Protein eIF4A.

Autor:	Tauber D; Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA., Tauber G; Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA., Khong A; Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA; Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, CO 80309, USA., Van Treeck B; Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA., Pelletier J; Department of Biochemistry, McGill University, Montreal, QC H3G 1Y6, Canada; The Rosalind and Morris Goodman Cancer Research Center and the Department of Oncology, McGill University, Montreal, QC, Canada., Parker R; Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA; Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, CO 80309, USA. Electronic address: roy.parker@colorado.edu.
Jazyk:	angličtina
Zdroj:	Cell [Cell] 2020 Feb 06; Vol. 180 (3), pp. 411-426.e16. Date of Electronic Publication: 2020 Jan 09.
DOI:	10.1016/j.cell.2019.12.031
Abstrakt:	Stress granules are condensates of non-translating mRNAs and proteins involved in the stress response and neurodegenerative diseases. Stress granules form in part through intermolecular RNA-RNA interactions, and to better understand how RNA-based condensation occurs, we demonstrate that RNA is effectively recruited to the surfaces of RNA or RNP condensates in vitro. We demonstrate that, through ATP-dependent RNA binding, the DEAD-box protein eIF4A reduces RNA condensation in vitro and limits stress granule formation in cells. This defines a function for eIF4A to limit intermolecular RNA-RNA interactions in cells. These results establish an important role for eIF4A, and potentially other DEAD-box proteins, as ATP-dependent RNA chaperones that limit the condensation of RNA, analogous to the function of proteins like HSP70 in combatting protein aggregates. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2020 Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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