Evidence map›Paper›PMID 41992520›Full record

ArticlePlant physiology2026

Chloroplastic protein PORC undergoes heat-induced condensation and enhances thermotolerance in Arabidopsis.

Fatema Alquraish, Israel Maruri-López, Marcin Luzarowski, Itzell E Hernández-Sánchez, Monika Chodasiewicz

Abstract read
In one paragraph

Article in Plant physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Fatema AlquraishBiological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 47000, Saudi Arabia.ORCID 0000-0001-6700-1524
Israel Maruri-LópezBiological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 47000, Saudi Arabia.
Marcin LuzarowskiCore Facility for Mass Spectrometry and Proteomics, Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.ORCID 0000-0002-2115-0468
Itzell E Hernández-SánchezBiological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 47000, Saudi Arabia.ORCID 0000-0001-6044-7240
Monika ChodasiewiczBiological and Environmental Science and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal 47000, Saudi Arabia.ORCID 0000-0002-0295-0638

Funding

CellNetworks Core Technology Platform (CCTP)Federal Ministry of Education and ResearchKAUSTMinistry of Science Baden WürttembergZMBH
6 · The paper itself

Abstract

Chloroplast stress granules (cpSGs) are emerging as dynamic suborganellar condensates that play a crucial role in mediating stress response in plants. In this study, we demonstrate that the chlorophyll biosynthesis enzyme protochlorophyllide oxidoreductase C (PORC) localizes to cpSGs in response to acute and prolonged heat stress in Arabidopsis (Arabidopsis thaliana). While PORC promoter activity was developmentally regulated and remained unresponsive to heat, PORC protein re-localized from a diffuse chloroplast distribution into punctate structures under elevated temperatures. This condensation was reversible, translation-dependent, and absent under optimal growth conditions. Genetic disruption of PORC resulted in compromised thermotolerance, whereas overexpression enhanced photosynthetic recovery following both acute (42 °C) and prolonged (35 °C) heat stress. High-throughput phenotyping and chlorophyll fluorescence imaging confirmed enhanced Photosystem II (PSII) efficiency and increased post-stress growth rate. Proteomic profiling of heat-induced PORC-cpSGs revealed functional enrichment of photosystem I/II components, proteases (eg, FtsH), and proteins involved in chlorophyll biosynthesis and photoprotection, suggesting a stress-protective role of cpSG under heat. These findings establish PORC as a key player in the chloroplast stress response, implicating cpSGs as protective hubs that facilitate the maintenance of photosynthetic integrity under elevated temperatures. Our study provides insight into chloroplast-specific biomolecular condensates, enhancing our understanding of plant stress resilience and paving the way for future studies on the regulation of their dynamics. Additionally, it highlights how components such as PORC could be utilized to develop heat-tolerant crops.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsThermotoleranceChlorophyllGene Expression Regulation, PlantHeat-Shock ResponseHot TemperatureOxidoreductases Acting on CH-CH Group DonorsPhotosynthesisPhotosystem II Protein ComplexStress, PhysiologicalArabidopsis ProteinsChlorophyllOxidoreductases Acting on CH-CH Group DonorsPhotosystem II Protein Complexprotochlorophyllide reductase

Identifiers

PMID41992520
PMCPMC13191595

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.