ArticleProceedings of the National Academy of Sciences of the United States of America2003
Induced nucleotide specificity in a GTPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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.
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Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Co-Translational Protein Folding and Sorting in Chloroplasts.Plants (Basel, Switzerland) · 2020Review
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- Protein translocation across the rough endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Article
- Translation elongation regulates substrate selection by the signal recognition particle.The Journal of biological chemistry · 2012Article
- Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA.PloS one · 2012Article
- Molecular mechanism of co-translational protein targeting by the signal recognition particle.Traffic (Copenhagen, Denmark) · 2011Review
- The crystal structure of the signal recognition particle in complex with its receptor.Science (New York, N.Y.) · 2011Article
- 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
- A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway.Molecular biology of the cell · 2009Article
- Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Biochemistry · 2009Article
- Distinct GDP/GTP bound states of the tandem G-domains of EngA regulate ribosome binding.Nucleic acids research · 2009Article
- Multiple conformational switches in a GTPase complex control co-translational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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- Article
- Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.The Journal of cell biology · 2007Article
- X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.PloS one · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
In signal-recognition particle (SRP)-dependent protein targeting to the bacterial plasma membrane, two GTPases, Ffh (a subunit of the bacterial SRP) and FtsY (the bacterial SRP receptor), act as GTPase activating proteins for one another. The molecular mechanism of this reciprocal GTPase activation is poorly understood. In this work, we show that, unlike other GTPases, free FtsY exhibits only low preference for GTP over other nucleotides. On formation of the SRP.FtsY complex, however, the nucleotide specificity of FtsY is enhanced 10(3)-fold. Thus, interactions with SRP must induce conformational changes that directly affect the FtsY GTP-binding site: in response to SRP binding, FtsY switches from a nonspecific "open" state to a "closed" state that provides discrimination between cognate and noncognate nucleotides. We propose that this conformational change leads to more accurate positioning of the nucleotide and thus could contribute to activation of FtsY's GTPase activity by a novel mechanism.
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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.