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Proteostatic tuning underpins the evolution of novel multicellular traits.

Kristopher MontroseDung T LacAnthony J BurnettiKai TongG Ozan BozdagMikaela HukkanenWilliam C RatcliffJuha Saarikangas
Published in: Science advances (2024)
The evolution of multicellularity paved the way for the origin of complex life on Earth, but little is known about the mechanistic basis of early multicellular evolution. Here, we examine the molecular basis of multicellular adaptation in the multicellularity long-term evolution experiment (MuLTEE). We demonstrate that cellular elongation, a key adaptation underpinning increased biophysical toughness and organismal size, is convergently driven by down-regulation of the chaperone Hsp90. Mechanistically, Hsp90-mediated morphogenesis operates by destabilizing the cyclin-dependent kinase Cdc28, resulting in delayed mitosis and prolonged polarized growth. Reinstatement of Hsp90 or Cdc28 expression resulted in shortened cells that formed smaller groups with reduced multicellular fitness. Together, our results show how ancient protein folding systems can be tuned to drive rapid evolution at a new level of biological individuality by revealing novel developmental phenotypes.
Keyphrases
  • heat shock protein
  • heat shock
  • cell cycle
  • heat stress
  • poor prognosis
  • induced apoptosis
  • genome wide
  • molecular dynamics simulations
  • tyrosine kinase
  • amino acid
  • signaling pathway
  • protein kinase