ArticleMolecular biology of the cell2007
Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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.
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.
Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- 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
- 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
- An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis.Protein science : a publication of the Protein Society · 2023Article
- Loss of CpFTSY Reduces Photosynthetic Performance and Affects Insertion of PsaC of PSI in Diatoms.Plant & cell physiology · 2023Article
- Post-translational regulation of metabolic checkpoints in plant tetrapyrrole biosynthesis.Journal of experimental botany · 2022Review
- How to Kinetically Dissect an RNA Machine.Biochemistry · 2021Article
- Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock.Nature plants · 2021Article
- 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
- 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
- Co-evolution of Two GTPases Enables Efficient Protein Targeting in an RNA-less Chloroplast Signal Recognition Particle Pathway.The Journal of biological chemistry · 2017Article
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- 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
- Article
- YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015Review
- A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.RNA (New York, N.Y.) · 2014Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cotranslational protein targeting to membranes is regulated by two GTPases in the signal recognition particle (SRP) and the SRP receptor; association between the two GTPases is slow and is accelerated 400-fold by the SRP RNA. Intriguingly, the otherwise universally conserved SRP RNA is missing in a novel chloroplast SRP pathway. We found that even in the absence of an SRP RNA, the chloroplast SRP and receptor GTPases can interact efficiently with one another; the kinetics of interaction between the chloroplast GTPases is 400-fold faster than their bacterial homologues, and matches the rate at which the bacterial SRP and receptor interact with the help of SRP RNA. Biochemical analyses further suggest that the chloroplast SRP receptor is pre-organized in a conformation that allows optimal interaction with its binding partner, so that conformational changes during complex formation are minimized. Our results highlight intriguing differences between the classical and chloroplast SRP and SRP receptor GTPases, and help explain how the chloroplast SRP pathway can mediate efficient targeting of proteins to the thylakoid membrane in the absence of the SRP RNA, which plays an indispensable role in all the other SRP pathways.
Indexed as
Identifiers
What OpenQuestion holds
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.