ArticleProceedings of the National Academy of Sciences of the United States of America1998
Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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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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
24 citing papers in PubMed, 59 citations in OpenAlex.
- Molecular Mechanisms of Priming Innate Immunity by Small Extracellular Vesicles Released during Infection with Gram-negative Bacteria.bioRxiv : the preprint server for biology · 2025Article
- The Passage of Chaperonins to Extracellular Locations inBiomolecules · 2025Article
- Characterization of Molecular Chaperone GroEL as a Potential Virulence Factor inFoods (Basel, Switzerland) · 2023Article
- Genome-wide CRISPRi screen identifies enhanced autolithotrophic phenotypes in acetogenic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Bordetella pertussis whole cell immunization protects against Pseudomonas aeruginosa infections.NPJ vaccines · 2022Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Growth phase-specific changes in the composition of E. coli transcription complexes.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- Structural Basis of the Subcellular Topology Landscape ofFrontiers in microbiology · 2019Article
- Physiology of the Inactivation of Vegetative Bacteria by Thermal Treatments: Mode of Action, Influence of Environmental Factors and Inactivation Kinetics.Foods (Basel, Switzerland) · 2017Review
- Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Scientific reports · 2015Article
- Complete genome determination and analysis of Acholeplasma oculi strain 19L, highlighting the loss of basic genetic features in the Acholeplasmataceae.BMC genomics · 2014Article
- The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles.Infection and immunity · 2012Article
- Activators of the glutamate-dependent acid resistance system alleviate deleterious effects of YidC depletion in Escherichia coli.Journal of bacteriology · 2011Article
- Consequences of depletion of the signal recognition particle in Escherichia coli.The Journal of biological chemistry · 2011Article
- Analysis of type II secretion of recombinant pneumococcal PspA and PspC in a Salmonella enterica serovar Typhimurium vaccine with regulated delayed antigen synthesis.Infection and immunity · 2008Article
- Characterization of an Escherichia coli O157:H7 plasmid O157 deletion mutant and its survival and persistence in cattle.Applied and environmental microbiology · 2007Article
- The Holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation.Journal of bacteriology · 2005Article
- A little help from my friends: quality control of presecretory proteins in bacteria.Journal of bacteriology · 2004Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperonin GroEL has been found to interact with isolated cytoplasmic membrane of Escherichia coli. Interaction requires Mg ions, whereas MgATP inhibits, and inhibition is stronger in the presence of co-chaperonin GroES. "Heat-shock" of the membrane at 45 degrees C destroys irreversibly its ability to bind GroEL. The binding of GroEL is characterized by saturation with a maximum of about 100 pmol GroEL bound per mg of total membrane protein, indicating a limited capacity and specificity of the membrane to bind GroEL. According to results of immunoblotting analysis and cleavable photoactivable cross-linking, a membrane target of GroEL is SecA, a protein known as a central component of the translocation machinery. Moreover, in some cases GroEL could modulate a cycle of association of SecA with the membrane by stimulating release of SecA from the membrane. A physiological role of targeting of GroEL in or close to the protein-conducting membrane apparatus is discussed.
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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.