A prion-like domain is required for phase separation and chloroplast RNA processing during cold acclimation in Arabidopsis

Plant Cell. 2024 Jul 31;36(8):2851-2872. doi: 10.1093/plcell/koae145.

Abstract

Arabidopsis (Arabidopsis thaliana) plants can produce photosynthetic tissue with active chloroplasts at temperatures as low as 4°C, and this process depends on the presence of the nuclear-encoded, chloroplast-localized RNA-binding protein CP29A. In this study, we demonstrate that CP29A undergoes phase separation in vitro and in vivo in a temperature-dependent manner, which is mediated by a prion-like domain (PLD) located between the two RNA recognition motif domains of CP29A. The resulting droplets display liquid-like properties and are found near chloroplast nucleoids. The PLD is required to support chloroplast RNA splicing and translation in cold-treated tissue. Together, our findings suggest that plant chloroplast gene expression is compartmentalized by inducible condensation of CP29A at low temperatures, a mechanism that could play a crucial role in plant cold resistance.

MeSH terms

  • Acclimatization* / genetics
  • Arabidopsis Proteins* / genetics
  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / genetics
  • Arabidopsis* / metabolism
  • Arabidopsis* / physiology
  • Chloroplasts* / metabolism
  • Cold Temperature*
  • Gene Expression Regulation, Plant
  • Phase Separation
  • Prions / genetics
  • Prions / metabolism
  • Protein Domains
  • RNA Splicing / genetics
  • RNA, Chloroplast* / genetics
  • RNA, Chloroplast* / metabolism
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism

Substances

  • Arabidopsis Proteins
  • RNA, Chloroplast
  • RNA-Binding Proteins
  • Prions