ArticleThe Journal of biological chemistry2010
cpSRP43 is a novel chaperone specific for light-harvesting chlorophyll a,b-binding proteins.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 59 citations in OpenAlex.
- 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
- The role of chloroplast SRP54 domains and its C-terminal tail region in post- and co-translational protein transport in vivo.Journal of experimental botany · 2024Article
- Simultaneous CAS9 editing of cpPlant direct · 2023Article
- cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach.Journal of chemical information and modeling · 2023Article
- Post-translational regulation of metabolic checkpoints in plant tetrapyrrole biosynthesis.Journal of experimental botany · 2022Review
- Comparative transcriptome analyses shed light on carotenoid production and plastid development in melon fruit.Horticulture research · 2021Article
- Go your own way: membrane-targeting sequences.Plant physiology · 2021Article
- Lasting consequences of psyllid (Bactericera cockerelli L.) infestation on tomato defense, gene expression, and growth.BMC plant biology · 2021Article
- Sexual and Apogamous Species of Woodferns Show Different Protein and Phytohormone Profiles.Frontiers in plant science · 2021Article
- Liquid-Liquid Phase Separation Phenomenon on Protein Sorting Within Chloroplasts.Frontiers in physiology · 2021Review
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- Two distinct sites of client protein interaction with the chaperone cpSRP43.The Journal of biological chemistry · 2018Article
- Complementation of a mutation in CpSRP43 causing partial truncation of light-harvesting chlorophyll antenna in Chlorella vulgaris.Scientific reports · 2017Article
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
- Sorting of SEC translocase SCY components to different membranes in chloroplasts.Journal of experimental botany · 2017Article
- Human cyclophilin 40 unravels neurotoxic amyloids.PLoS biology · 2017Article
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- Design and engineering of water-soluble light-harvesting protein maquettes.Chemical science · 2017Article
- Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biosynthesis of most membrane proteins is directly coupled to membrane insertion, and therefore, molecular chaperones are not required. The light-harvesting chlorophyll a,b-binding proteins (LHCPs) present a prominent exception as they are synthesized in the cytoplasm, and after import into the chloroplast, they are targeted and inserted into the thylakoid membrane. Upon arrival in the stroma, LHCPs form a soluble transit complex with the chloroplast signal recognition particle (cpSRP) consisting of an SRP54 homolog and the unique cpSRP43 composed of three chromodomains and four ankyrin repeats. Here we describe that cpSRP43 alone prevents aggregation of LHCP by formation of a complex with nanomolar affinity, whereas cpSRP54 is not required for this chaperone activity. Other stromal chaperones like trigger factor cannot replace cpSRP43, which implies that LHCPs require a specific chaperone. Although cpSRP43 does not have an ATPase activity, it can dissolve aggregates of LHCPs similar to chaperones of the Hsp104/ClpB family. We show that the LHCP-cpSRP43 interaction is predominantly hydrophobic but strictly depends on an intact DPLG motif between the second and third transmembrane region. The cpSRP43 ankyrin repeats that provide the binding site for the DPLG motif are sufficient for the chaperone function, whereas the chromodomains are dispensable. Taken together, we define cpSRP43 as a highly specific chaperone for LHCPs in addition to its established function as a targeting factor for this family of membrane proteins.
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