ArticleThe Journal of biological chemistry2015
Chloroplast SRP54 Was Recruited for Posttranslational Protein Transport via Complex Formation with Chloroplast SRP43 during Land Plant Evolution.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Structure, function, and assembly of PSI in thylakoid membranes of vascular plants.The Plant cell · 2024Review
- 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
- Diversification of Plastid Structure and Function in Land Plants.Methods in molecular biology (Clifton, N.J.) · 2024Article
- PALE-GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI-LHCI supercomplex.Plant direct · 2022Article
- Impact of Porphyrin Binding to GENOMES UNCOUPLED 4 on Tetrapyrrole BiosynthesisFrontiers in plant science · 2022Article
- Identification and characterization ofHorticulture research · 2022Article
- A homolog of GuidedEntry of Tail-anchored proteins3 functions in membrane-specific protein targeting in chloroplasts of Arabidopsis.The Plant cell · 2021Article
- SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.International journal of molecular sciences · 2021Review
- Protein Targeting Into the Thylakoid Membrane Through Different Pathways.Frontiers in physiology · 2021Review
- Chloroplast SRP54s are Essential for Chloroplast Development in Rice.Rice (New York, N.Y.) · 2020Article
- Co-Translational Protein Folding and Sorting in Chloroplasts.Plants (Basel, Switzerland) · 2020Review
- Ribosome-Associated Chloroplast SRP54 Enables Efficient Cotranslational Membrane Insertion of Key Photosynthetic Proteins.The Plant cell · 2019Article
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Chloroplast PetD protein: evidence for SRP/Alb3-dependent insertion into the thylakoid membrane.BMC plant biology · 2017Article
- Co-evolution of Two GTPases Enables Efficient Protein Targeting in an RNA-less Chloroplast Signal Recognition Particle Pathway.The Journal of biological chemistry · 2017Article
- Article
- Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.The Journal of biological chemistry · 2015Article
- Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.Nature communications · 2015Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, membrane proteins are targeted cotranslationally via a signal recognition particle (SRP). During the evolution of higher plant chloroplasts from cyanobacteria, the SRP pathway underwent striking adaptations that enable the posttranslational transport of the abundant light-harvesting chlorophyll-a/b-binding proteins (LHCPs). The conserved 54-kDa SRP subunit in higher plant chloroplasts (cpSRP54) is not bound to an SRP RNA, an essential SRP component in bacteria, but forms a stable heterodimer with the chloroplast-specific cpSRP43. This heterodimeric cpSRP recognizes LHCP and delivers it to the thylakoid membrane whereby cpSRP43 plays a central role. This study shows that the cpSRP system in the green alga Chlamydomonas reinhardtii differs significantly from that of higher plants as cpSRP43 is not complexed to cpSRP54 in Chlamydomonas and cpSRP54 is not involved in LHCP recognition. This divergence is attributed to altered residues within the cpSRP54 tail and the second chromodomain of cpSRP43 that are crucial for the formation of the binding interface in Arabidopsis. These changes are highly conserved among chlorophytes, whereas all land plants contain cpSRP proteins with typical interaction motifs. These data demonstrate that the coevolution of LHCPs and cpSRP43 occurred independently of complex formation with cpSRP54 and that the interaction between cpSRP54 and cpSRP43 evolved later during the transition from chlorophytes to land plants. Furthermore, our data show that in higher plants a heterodimeric form of cpSRP is required for the formation of a low molecular weight transit complex with LHCP.
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