ArticleThe EMBO journal2001
Evidence for a novel GTPase priming step in the SRP protein targeting pathway.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 41 citations in OpenAlex.
- 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
- SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Nature structural & molecular biology · 2008Article
- The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.Molecular biology of the cell · 2007Article
- X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.Proteins · 2007Article
- Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites.The Journal of cell biology · 2006Article
- Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.Arthritis research & therapy · 2006Article
- FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon.EMBO reports · 2005Article
- Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Mechanism of association and reciprocal activation of two GTPases.PLoS biology · 2004Article
- Article
- Heterodimeric GTPase core of the SRP targeting complex.Science (New York, N.Y.) · 2004Article
- Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.Acta crystallographica. Section D, Biological crystallography · 2003Article
- The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome.RNA (New York, N.Y.) · 2003Article
- Induced nucleotide specificity in a GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Role for both DNA and RNA in GTP hydrolysis by the Neisseria gonorrhoeae signal recognition particle receptor.Journal of bacteriology · 2003Article
- Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh.Journal of molecular biology · 2002Article
- Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY.Biochimica et biophysica acta · 2002Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Protein targeting by the signal recognition particle (SRP) pathway requires the interaction of two homologous GTPases that reciprocally regulate each other's GTPase activity, the SRP signal peptide- binding subunit (SRP54) and the SRP receptor alpha-subunit (SRalpha). The GTPase domain of both proteins abuts a unique 'N domain' that appears to facilitate external ligand binding. To examine the relationship between the unusual regulation and unique architecture of the SRP pathway GTPases, we mutated an invariant glycine in Escherichia coli SRP54 and SRalpha orthologs ('Ffh' and 'FtsY', respectively) that resides at the N-GTPase domain interface. A G257A mutation in Ffh produced a lethal phenotype. The mutation did not significantly affect Ffh function, but severely reduced interaction with FtsY. Likewise, mutation of FtsY Gly455 produced growth defects and inhibited interaction with Ffh. The data suggest that Ffh and FtsY interact only in a 'primed' conformation which requires interdomain communication. Based on these results, we propose that the distinctive features of the SRP pathway GTPases evolved to ensure that SRP and the SR engage external ligands before interacting with each other.
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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.