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7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress

Author

Listed:
  • Bojan Bujisic

    (Massachusetts General Hospital
    Harvard Medical School)

  • Hun-Goo Lee

    (Massachusetts General Hospital
    Harvard Medical School)

  • Lilei Xu

    (Massachusetts General Hospital
    Harvard Medical School)

  • Uri Weissbein

    (Massachusetts General Hospital
    Harvard Medical School)

  • Carlos Rivera

    (Massachusetts General Hospital
    Harvard Medical School)

  • Ivan Topisirovic

    (McGill University)

  • Jeannie T. Lee

    (Massachusetts General Hospital
    Harvard Medical School)

Abstract

Non-coding 7SL RNA is an ancestor to mammalian Alu and B1 SINE RNAs and is thought to function exclusively within the Signal Recognition Particle (SRP), aiding in the translocation of secretory proteins into the endoplasmic reticulum for export. Here, we discover a function of 7SL/SRP unrelated to protein secretion. Under acute heat shock, 7SL and SRP together selectively arrest cellular transcription and translation machineries during early response to stress. Under thermal stress, 7SL is upregulated, accumulates in the nucleus, and binds to target genes repressed by heat shock. Concurrently, in the cytosol, SRP binds to ribosomes and inhibits new protein synthesis. Translational suppression occurs independently of the signal peptide and is abrogated by depleting SRP. Translation inhibition extends to the mitochondria, as nuclear-encoded genes with mitochondrial functions are enriched among SRP targets. Thus, apart from its role in protein export, 7SL/SRP orchestrates a global response to acute stress that encompasses the nucleus, cytosol, and mitochondria across transcription and translation.

Suggested Citation

  • Bojan Bujisic & Hun-Goo Lee & Lilei Xu & Uri Weissbein & Carlos Rivera & Ivan Topisirovic & Jeannie T. Lee, 2025. "7SL RNA and signal recognition particle orchestrate a global cellular response to acute thermal stress," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56351-6
    DOI: 10.1038/s41467-025-56351-6
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    References listed on IDEAS

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    1. Changhe Ji & Jakob Bader & Pradhipa Ramanathan & Luisa Hennlein & Felix Meissner & Sibylle Jablonka & Matthias Mann & Utz Fischer & Michael Sendtner & Michael Briese, 2021. "Interaction of 7SK with the Smn complex modulates snRNP production," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Justin W. Chartron & Katherine C. L. Hunt & Judith Frydman, 2016. "Cotranslational signal-independent SRP preloading during membrane targeting," Nature, Nature, vol. 536(7615), pages 224-228, August.
    3. Mario Halic & Thomas Becker & Martin R. Pool & Christian M. T. Spahn & Robert A. Grassucci & Joachim Frank & Roland Beckmann, 2004. "Structure of the signal recognition particle interacting with the elongation-arrested ribosome," Nature, Nature, vol. 427(6977), pages 808-814, February.
    4. Matthew D. Simon & Stefan F. Pinter & Rui Fang & Kavitha Sarma & Michael Rutenberg-Schoenberg & Sarah K. Bowman & Barry A. Kesner & Verena K. Maier & Robert E. Kingston & Jeannie T. Lee, 2013. "High-resolution Xist binding maps reveal two-step spreading during X-chromosome inactivation," Nature, Nature, vol. 504(7480), pages 465-469, December.
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