ArticleNature plants2021
Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock.
Article in Nature plants, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 46 citations in OpenAlex.
- Design Principles of Plant Thermotolerance: Integrating Photosynthesis, Reproduction, and Field Resilience in a Warming Climate.Plant, cell & environment · 2026Review
- Convergent roles of BcGUN4.1, BcSG1, BcCHLH, and BcTPR4 in regulating the leaf greenness of non-heading Chinese cabbage.Molecular horticulture · 2026Article
- Heat Shock Transcription Factor OsHsfc1a Enhances Rice Seedling Thermotolerance by Regulating OsMFT1 and Preserving Chloroplast Structure Under Heat Stress.Plant biotechnology journal · 2026Article
- Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Molecular Networks Governing Plant Responses to Heat and Cold Stress.Plants (Basel, Switzerland) · 2025Review
- Switchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.Science advances · 2025Article
- Coordinated cpSRP43 and cpSRP54 Abundance Is Essential for Tetrapyrrole Biosynthesis While cpSRP43 Is Independent of Retrograde Signaling.Plants (Basel, Switzerland) · 2025Article
- Structural and mechanistic basis for the regulation of the chloroplast signal recognition particle by (p)ppGpp.FEBS letters · 2025Article
- LTD coordinates chlorophyll biosynthesis and LIGHT-HARVESTING CHLOROPHYLL A/B-BINDING PROTEIN transport.The Plant cell · 2025Article
- Regulatory and retrograde signaling networks in the chlorophyll biosynthetic pathway.Journal of integrative plant biology · 2025Review
- Morphological, Physiological, and Molecular Responses to Heat Stress in Brassicaceae.Plants (Basel, Switzerland) · 2025Review
- Modification of aggregation-prone regions of Arabidopsis glutamyl-tRNA reductase leads to increased stability while maintaining enzyme activity.Frontiers in plant science · 2025Article
- Adaptive responses of plants to light stress: mechanisms of photoprotection and acclimation. A review.Frontiers in plant science · 2025Review
- STIC2 selectively binds ribosome-nascent chain complexes in the cotranslational sorting of Arabidopsis thylakoid proteins.The EMBO journal · 2024Article
- Article
- An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis.Protein science : a publication of the Protein Society · 2023Article
- Rice HEAT SHOCK PROTEIN60-3B maintains male fertility under high temperature by starch granule biogenesis.Plant physiology · 2023Article
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- Fine mapping of CscpFtsY, a gene conferring the yellow leaf phenotype in cucumber (Cucumis sativus L.).BMC plant biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The assembly of light-harvesting chlorophyll-binding proteins (LHCPs) is coordinated with chlorophyll biosynthesis during chloroplast development. The ATP-independent chaperone known as chloroplast signal recognition particle 43 (cpSRP43) mediates post-translational LHCP targeting to the thylakoid membrane and also participates in tetrapyrrole biosynthesis (TBS). How these distinct actions of cpSRP43 are controlled has remained unclear. Here, we demonstrate that cpSRP43 effectively protects several TBS proteins from heat-induced aggregation and enhances their stability during leaf greening and heat shock. While the substrate-binding domain of cpSRP43 is sufficient for chaperoning LHCPs, the stabilization of TBS clients requires the chromodomain 2 of the protein. Strikingly, cpSRP54-which activates cpSRP43's LHCP-targeted function-inhibits the chaperone activity of cpSRP43 towards TBS proteins. High temperature weakens the interaction of cpSRP54 with cpSRP43, thus freeing cpSRP43 to interact with and protect the integrity of TBS proteins. Our data indicate that the temperature sensitivity of the cpSRP43-cpSRP54 complex enables cpSRP43 to serve as an autonomous chaperone for the thermoprotection of TBS proteins.
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Registered trials
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.