ReviewCurrent genetics2004
Structure and function of the chloroplast signal recognition particle.
Review in Current genetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 97 citations in OpenAlex.
- Chloroplast SRP54 and FtsH protease coordinate thylakoid membrane-associated proteostasis in Arabidopsis.Plant physiology · 2023Article
- PALE-GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI-LHCI supercomplex.Plant direct · 2022Article
- Transcriptome Analyses of Near Isogenic Lines Reveal Putative Drought Tolerance Controlling Genes in Wheat.Frontiers in plant science · 2022Article
- Get closer and make hotspots: liquid-liquid phase separation in plants.EMBO reports · 2021Review
- A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone.Journal of molecular biology · 2020Article
- 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
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
- Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.Biophysical journal · 2016Article
- 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
- Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.Nature communications · 2015Article
- Ribosome nascent chain complexes of the chloroplast-encoded cytochrome b6 thylakoid membrane protein interact with cpSRP54 but not with cpSecY.Journal of bioenergetics and biomembranes · 2015Article
- Proteins affecting thylakoid morphology - the key to understanding vesicle transport in chloroplasts?Plant signaling & behavior · 2014Article
- YGL138(t), encoding a putative signal recognition particle 54 kDa protein, is involved in chloroplast development of rice.Rice (New York, N.Y.) · 2013Article
- The protein translocation systems in plants - composition and variability on the example of Solanum lycopersicum.BMC genomics · 2013Article
- How to build functional thylakoid membranes: from plastid transcription to protein complex assembly.Planta · 2013Review
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid membrane.Plant molecular biology · 2011Article
- LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway.Nature communications · 2011Article
- The GDC1 gene encodes a novel ankyrin domain-containing protein that is essential for grana formation in Arabidopsis.Plant physiology · 2011Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The targeting of proteins, including the insertion and translocation of proteins in or across membranes, is a fundamental process within a cell, and a variety of specialized mechanisms for protein transport have been developed during evolution. The signal recognition particle (SRP) is found in the cytoplasm of most, if not all, eukaryotes and prokaryotes where it plays a central role in the co-translational insertion of membrane proteins into the endoplasmic reticulum and plasma membrane, respectively. SRP is a ribonucleoprotein consisting of an RNA and at least one polypeptide of approximately 54 kDa (SRP54). Interestingly, chloroplasts contain a specialized type of signal recognition particle. Chloroplast SRP (cpSRP) contains a SRP54 homologue but differs strikingly from cytosolic SRP in various aspects of structure and function. In contrast to cytosolic SRP, it contains a novel protein subunit (cpSRP43) and lacks RNA. CpSRP is also distinctive in its ability to interact with its substrate, light-harvesting chlorophyll a/ b-binding protein, post-translationally. Furthermore, it is remarkable that the 54 kDa subunit of cpSRP is also involved in the co-translational transport of chloroplast-encoded thylakoid proteins, and is therefore able to switch between the co- and post-translational means of interaction with its respective substrate proteins.
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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.