ArticleRNA (New York, N.Y.)2009
Conformation of the signal recognition particle in ribosomal targeting complexes.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.Biophysical journal · 2016Article
- 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
- Dynamic switch of the signal recognition particle from scanning to targeting.Nature structural & molecular biology · 2012Article
- Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.Molecular biology of the cell · 2011Article
- Inhibitors of MAPK pathway ERK1/2 or p38 prevent the IL-1{beta}-induced up-regulation of SRP72 autoantigen in Jurkat cells.The Journal of biological chemistry · 2010Article
- GTPases and the origin of the ribosome.Biology direct · 2010Article
- Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.BMC biology · 2009Article
- The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins.Nature structural & molecular biology · 2009Review
- Delivering proteins for export from the cytosol.Nature reviews. Molecular cell biology · 2009Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial signal recognition particle (SRP) binds to ribosomes synthesizing inner membrane proteins and, by interaction with the SRP receptor, FtsY, targets them to the translocon at the membrane. Here we probe the conformation of SRP and SRP protein, Ffh, at different stages of targeting by measuring fluorescence resonance energy transfer (FRET) between fluorophores placed at various positions within SRP. Distances derived from FRET indicate that SRP binding to nontranslating ribosomes triggers a global conformational change of SRP that facilitates binding of the SRP receptor, FtsY. Binding of SRP to a signal-anchor sequence exposed on a ribosome-nascent chain complex (RNC) causes a further change of the SRP conformation, involving the flexible part of the Ffh(M) domain, which increases the affinity for FtsY of ribosome-bound SRP up to the affinity exhibited by the isolated NG domain of Ffh. This indicates that in the RNC-SRP complex the Ffh(NG) domain is fully exposed for binding FtsY to form the targeting complex. Binding of FtsY to the RNC-SRP complex results in a limited conformational change of SRP, which may initiate subsequent targeting steps.
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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.