ArticleBiochimica et biophysica acta2002
Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY.
Article in Biochimica et biophysica acta, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- 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
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle.Biochemistry · 2011Article
- Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.The Journal of cell biology · 2010Article
- Archaea signal recognition particle shows the way.Archaea (Vancouver, B.C.) · 2010Review
- A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway.Molecular biology of the cell · 2009Article
- The distinct anchoring mechanism of FtsY from different microbes.Current microbiology · 2009Article
- Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Biochemistry · 2009Article
- SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Nature structural & molecular biology · 2008Article
- FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor.Current microbiology · 2008Article
- Article
- 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
- X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.PloS one · 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
- Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.Journal of structural biology · 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
- Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site.Journal of molecular biology · 2006Article
- 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
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The structural basis for the GTP-dependent co-translational targeting complex between the signal recognition particle (SRP) and its receptor is unknown. The complex has been shown to have unusual kinetics of formation, and association in vivo is likely to be dependent on catalysis by the SRP RNA. We have determined conditions for RNA-independent association of the 'NG' GTPase domains of the prokaryotic homologs of the SRP components, Ffh and FtsY, from Thermus aquaticus. Consistent with previous studies of the Escherichia coli proteins, the kinetics of association and dissociation are slow. The T. aquaticus FtsY is sensitive to an endogenous proteolytic activity that cleaves at two sites--the first in a lengthy linker peptide that spans the interface between the N and G domains, and the second near the N-terminus of the N domain of FtsY. Remarkably, this second cleavage occurs only on formation of the Ffh/FtsY complex. The change in protease sensitivity of this region, which is relatively unstructured in the FtsY but not in the Ffh NG domain, implies that it undergoes conformational change on formation of the complex between the two proteins. The N domain, therefore, participates in the interactions that mediate the GTP-dependent formation of the targeting complex.
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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.