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Modulation of RNA condensation by the DEAD-box protein eIF4A

Devin Tauber, Gabriel Tauber, Anthony Khong, Briana Van Treeck, Jerry Pelletier, Roy Parker
doi: https://doi.org/10.1101/689802
Devin Tauber
1Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA
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Gabriel Tauber
1Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA
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Anthony Khong
1Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA
2Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, CO 80309, USA
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Briana Van Treeck
1Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA
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Jerry Pelletier
3Department 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
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Roy Parker
1Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, USA
2Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, CO 80309, USA
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  • For correspondence: roy.parker@colorado.edu
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SUMMARY

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, although the process of RNA condensation is poorly understood. In vitro, we demonstrate that RNA is effectively recruited to the surfaces of RNA or RNP condensates. We demonstrate that the DEAD-box protein eIF4A reduces RNA condensation in vitro and limits stress granule formation in cells. This defines a purpose for eIF4A to limit intermolecular RNA-RNA interactions in cells, thereby allowing for proper RNP function. These results establish an important role for DEAD-box proteins as ATP-dependent RNA chaperones that can limit the intermolecular condensation and entanglement of RNA, analogous to the function of proteins like HSP70 in combatting protein aggregates.

eTOC Blurb Stress granules are formed in part by the process of RNA condensation, which is mediated by and promotes trans RNA-RNA interactions. The essential DEAD-box protein and translation initiation factor eIF4A limits stress granule formation by reducing RNA condensation through its function as an ATP-dependent RNA binding protein, behaving analogously to how protein chaperones like HSP70 combat protein aggregates.

Highlights

  • RNA condensates promote intermolecular RNA-RNA interactions at their surfaces

  • eIF4A limits the recruitment of RNAs to stress granules in cells

  • eIF4A reduces the nucleation of stress granules in cells

  • Recombinant eIF4A1 inhibits the condensation of RNA in vitro in an ATP-dependent manner

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted November 07, 2019.
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Modulation of RNA condensation by the DEAD-box protein eIF4A
Devin Tauber, Gabriel Tauber, Anthony Khong, Briana Van Treeck, Jerry Pelletier, Roy Parker
bioRxiv 689802; doi: https://doi.org/10.1101/689802
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Modulation of RNA condensation by the DEAD-box protein eIF4A
Devin Tauber, Gabriel Tauber, Anthony Khong, Briana Van Treeck, Jerry Pelletier, Roy Parker
bioRxiv 689802; doi: https://doi.org/10.1101/689802

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