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Solid-like condensation of MORF8 inhibits RNA editing under heat stress in Arabidopsis

ABSTRACT: Heat stress inhibits photosynthesis efficiency, thereby suppressing plant growth and crop yield. However, the mechanism underlying this inhibition is not fully understood. Here, we report that the multiple organellar RNA-editing factor 8 (MORF8) forms condensates with solid-like properties in chloroplast upon heat stress. In vitro data show that the MORF8 condensation is intrinsically heat-dependent and primarily determined by its IDR (intrinsically disordered region). Purification and characterization of MORF8 condensates show that numerous editing factors including PPR proteins and MORFs are partitioned. We provide both genetic and biochemical evidence that MORF8 condensation inhibits chloroplast RNA editing. In agreement, we find that both heat stress and MORF8 condensation lead to reduced editing of RNAs encoding NADH dehydrogenase-like (NDH) complex and impaired NDH activity and photosynthesis efficiency. These findings uncover MORF8 as a putative chloroplastic thermosensor that mediates photosynthesis inhibition by heat and highlight the functional significance of solid material properties of biomolecular condensates.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Jie Wu

LAB HEAD: Xiaofeng Fang

PROVIDER: PXD061133 | Pride | 2025-03-07

REPOSITORIES: pride

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Project description:Cellular responses to maladaptive environmental changes—stresses—allow for organismal adaptation to diverse and dynamic conditions. Across the tree of life, cells upregulate a highly conserved transcriptional program in response to so-called proteotoxic stresses such as heat shock. Correspondingly, in eukaryotes, these stresses induce the formation of biomolecular condensates, clusters of mRNA and protein which are referred to as stress granules under severe stress. However, major questions remain about this stress-induced response. How conserved is the condensation response relative to the transcriptional response? How does it vary across environmental niches, and to what extent does it correspond with the conserved transcriptional response? To answer these fundamental questions, we studied the growth, transcriptional, and condensation heat-induced stress responses in three fungal species adapted to thrive in different thermal environments: cryophilic S. kudriavzevii, mesophilic S. cerevisiae, and thermotolerant K. marxianus. Here we show that transcriptional heat shock responses track each species’ evolved temperature range of growth. Further, orthologous proteins—including poly(A)-binding protein, Pab1, a core marker of stress granules—form condensates in vivo at temperatures systematically tuned to the temperature at which the organisms activate the transcriptional heat shock response and slow their growth. In vitro, purified Pab1 from each species condenses autonomously at niche-specific temperatures. Homologous mutations in Pab1 cause similar shifts in relative condensation temperature across species, and crucially, mutations which suppress condensation in vitro also reduce fitness during heat stress. Our findings indicate that stress-induced protein condensation is adaptive, conserved, integrated with the growth and transcriptional responses, and tuned to features of the cellular and organismal environment to initiate at niche-specific levels.

			Action	DRS
	MS241465-42-1.msf	Msf
	MS241465-42-1.mzML	Mzml
	MS241465-42-1.mzTab	Mztab
	MS241465-42-1.raw	Raw
	MS241465-42-2.msf	Msf

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Solid-like condensation of MORF8 inhibits RNA editing under heat stress in Arabidopsis

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