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

Author:

Legen Julia1ORCID,Lenzen Benjamin1ORCID,Kachariya Nitin23ORCID,Feltgen Stephanie1ORCID,Gao Yang4ORCID,Mergenthal Simon5ORCID,Weber Willi5ORCID,Klotzsch Enrico5ORCID,Zoschke Reimo4ORCID,Sattler Michael23ORCID,Schmitz-Linneweber Christian1ORCID

Affiliation:

1. Molecular Genetics, Humboldt Universität zu Berlin , Philippstrasse 13, Berlin 10115 , Germany

2. Helmholtz Munich, Institute of Structural Biology , Ingolstädter Landstrasse 1, Munich 85764 , Germany

3. Department of Bioscience, Bavarian NMR Center, TUM School of Natural Sciences, Technical University of Munich , Lichtenbergstrasse 4, Garching 85747 , Germany

4. Max Planck Institute of Molecular Plant Physiology , Am Mühlenberg 1, Potsdam-Golm 14476 , Germany

5. Institute for Biology, Experimental Biophysics/Mechanobiology, Humboldt-Universität zu Berlin , Invalidenstrasse 42, Berlin 10115 , Germany

Abstract

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.

Funder

DFG

C.S.

C.S.. and M.S.

Publisher

Oxford University Press (OUP)

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