Efficient translation of chaperones by eIF5A safeguards proteostasis under heat stress

In yeast, eIF5A is required for a rapid heat-stress response, preventing ribosome stalling and enabling efficient synthesis of high codon-optimal chaperones like Hsp70 Ssa1 and Hsp12.

• Why it matters: Heat disrupts proteostasis, but how cells rapidly boost chaperone production during stress is not fully understood.
• What they did: Yeast lacking eIF5A shows ribosome stalling on heat-induced mRNAs, with reduced chaperone translation; eIF5A preferentially associates with high codon-optimal induced mRNAs and its polysome association increases under heat shock.
• The result: Low Hsp70 in eIF5A mutants delays Hsf1 feedback inhibition during stress adaptation and leads to protein aggregate accumulation, lowering viability under heat stress.

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