ArticleJournal of bacteriology2002
Functional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 30 citations in OpenAlex.
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
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- Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.Journal of bacteriology · 2020Article
- Differential expression pattern of the proteome in response to cadmium stress based on proteomics analysis of wheat roots.BMC genomics · 2020Article
- Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis.Molecular & cellular proteomics : MCP · 2012Article
- Article
- Article
- Identification of candidate structured RNAs in the marine organism 'Candidatus Pelagibacter ubique'.BMC genomics · 2009Article
- Characterization of conserved bases in 4.5S RNA of Escherichia coli by construction of new F' factors.Journal of bacteriology · 2008Article
- Article
- SecY alterations that impair membrane protein folding and generate a membrane stress.The Journal of cell biology · 2007Article
- Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane.Journal of bacteriology · 2005Article
- Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli.The EMBO journal · 2004Article
- Ligand crowding at a nascent signal sequence.The Journal of cell biology · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Ffh protein of Escherichia coli is a 48-kDa polypeptide that is homologous to the SRP54 subunit of the eukaryotic signal recognition particle (SRP). Efforts to understand the function of Ffh in bacteria have depended largely on the use of E. coli strains that allow depletion of the wild-type gene product. As an alternative approach to studying Ffh, a temperature-sensitive ffh mutant was isolated. The ffh-10(Ts) mutation results in two amino acid changes in conserved regions of the Ffh protein, and characterization of the mutant revealed that the cells rapidly lose viability at the nonpermissive temperature of 42 degrees C as well as show reduced growth at the permissive temperature of 30 degrees C. While the ffh mutant is defective in insertion of inner membrane proteins, the export of proteins with cleavable signal sequences is not impaired. The mutant also shows elevated expression of heat shock proteins and accumulates insoluble proteins, especially at 42 degrees C. It was further observed that the temperature sensitivity of the ffh mutant was suppressed by overproduction of 4.5S RNA, the RNA component of the bacterial SRP, by stabilizing the thermolabile protein. Collectively, these results are consistent with a model in which Ffh is required only for localization of proteins integral to the cytoplasmic membrane and suggest new genetic approaches to the study of how the structure of the SRP contributes to its function.
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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.