ArticlePLoS biology2004
Mechanism of association and reciprocal activation of two GTPases.
Article in PLoS biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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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
63 citing papers in PubMed, 105 citations in OpenAlex.
- Temporal Regulation of Signal Recognition Particle During Translation.Journal of molecular biology · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- 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
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Genome-wide insights into population structure and host specificity of Campylobacter jejuni.Scientific reports · 2021Article
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- GTP-Dependent FlhF Homodimer Supports Secretion of a Hemolysin inFrontiers in microbiology · 2020Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- Article
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Co-evolution of Two GTPases Enables Efficient Protein Targeting in an RNA-less Chloroplast Signal Recognition Particle Pathway.The Journal of biological chemistry · 2017Article
- Analysis of the GTPase motif of FlhF in the control of the number and location of polar flagella inBiophysics and physicobiology · 2017Article
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity.The Journal of biological chemistry · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
3 more citing papers are in PubMed but not listed here.
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The signal recognition particle (SRP) mediates the cotranslational targeting of nascent proteins to the eukaryotic endoplasmic reticulum membrane or the bacterial plasma membrane. During this process, two GTPases, one in SRP and one in the SRP receptor (named Ffh and FtsY in bacteria, respectively), form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Here, we explore by site-directed mutagenesis the role of 45 conserved surface residues in the Ffh-FtsY interaction. Mutations of a large number of residues at the interface impair complex formation, supporting the importance of an extensive interaction surface. Surprisingly, even after a stable complex is formed, single mutations in FtsY can block the activation of GTP hydrolysis in both active sites. Thus, activation requires conformational changes across the interface that coordinate the positioning of catalytic residues in both GTPase sites. A distinct class of mutants exhibits half-site reactivity and thus allows us to further uncouple the activation of individual GTPases. Our dissection of the activation process suggests discrete conformational stages during formation of the active SRP*SRP receptor complex. Each stage provides a potential control point in the targeting reaction at which regulation by additional components can be exerted, thus ensuring the binding and release of cargo at the appropriate time.
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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.