ArticleMolecular biology of the cell2009
A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- 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
- Molecular mechanism of SRP-dependent light-harvesting protein transport to the thylakoid membrane in plants.Photosynthesis research · 2018Review
- 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
- Article
- Structural diversity of signal recognition particle RNAs in plastids.Plant signaling & behavior · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Article
- Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle.Biochemistry · 2011Article
- A dynamic cpSRP43-Albino3 interaction mediates translocase regulation of chloroplast signal recognition particle (cpSRP)-targeting components.The Journal of biological chemistry · 2010Article
- Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane.The Journal of biological chemistry · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cotranslational protein targeting by the signal recognition particle (SRP) requires the SRP RNA, which accelerates the interaction between the SRP and SRP receptor 200-fold. This otherwise universally conserved SRP RNA is missing in the chloroplast SRP (cpSRP) pathway. Instead, the cpSRP and cpSRP receptor (cpFtsY) by themselves can interact 200-fold faster than their bacterial homologues. Here, cross-complementation analyses revealed the molecular origin underlying their efficient interaction. We found that cpFtsY is 5- to 10-fold more efficient than Escherichia coli FtsY at interacting with the GTPase domain of SRP from both chloroplast and bacteria, suggesting that cpFtsY is preorganized into a conformation more conducive to complex formation. Furthermore, the cargo-binding M-domain of cpSRP provides an additional 100-fold acceleration for the interaction between the chloroplast GTPases, functionally mimicking the effect of the SRP RNA in the cotranslational targeting pathway. The stimulatory effect of the SRP RNA or the M-domain of cpSRP is specific to the homologous SRP receptor in each pathway. These results strongly suggest that the M-domain of SRP actively communicates with the SRP and SR GTPases and that the cytosolic and chloroplast SRP pathways have evolved distinct molecular mechanisms (RNA vs. protein) to mediate this communication.
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