ArticleJournal of bacteriology1994
Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity.
Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 80 citations in OpenAlex.
- Origin and Evolution of Bacterial Periplasmic Force Transducers.Molecular biology and evolution · 2025Article
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- TrhA, a bacterial progestin and adiponectin receptor homolog, couples membrane energetics homeostasis and unsaturated fatty acid metabolism.Journal of bacteriology · 2024Article
- Article
- Force-Generation by the Trans-Envelope Tol-Pal System.Frontiers in microbiology · 2022Review
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- Decoupling Filamentous Phage Uptake and Energy of the TolQRA Motor in Escherichia coli.Journal of bacteriology · 2020Article
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Polar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complex.Molecular microbiology · 2014Article
- Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway.Journal of bacteriology · 2013Article
- Mapping the interactions between Escherichia coli TolQ transmembrane segments.The Journal of biological chemistry · 2011Article
- The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor.Journal of bacteriology · 2010Article
- Cell envelope perturbation induces oxidative stress and changes in iron homeostasis in Vibrio cholerae.Journal of bacteriology · 2009Article
- Genome-wide screens: novel mechanisms in colicin import and cytotoxicity.Molecular microbiology · 2009Article
- Toxicogenomic response of Pseudomonas aeruginosa to ortho-phenylphenol.BMC genomics · 2008Article
- Interactions of the energy transducer TonB with noncognate energy-harvesting complexes.Journal of bacteriology · 2008Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Defective O-antigen polymerization in tolA and pal mutants of Escherichia coli in response to extracytoplasmic stress.Journal of bacteriology · 2005Article
- Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12.Journal of bacteriology · 2004Article
- Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB.Journal of bacteriology · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
TolQ is a 230-amino-acid protein required to maintain the integrity of the bacterial envelope and to facilitate the import of both filamentous bacteriophage and group A colicins. Cellular fractionation experiments showed TolQ to be localized to the cytoplasmic membrane. Bacteria expressing a series of TolQ-beta-galactosidase and TolQ-alkaline phosphatase fusion proteins were analyzed for the appropriate enzyme activity, membrane location, and sensitivity to exogenously added protease. The results are consistent with TolQ being an integral cytoplasmic membrane protein with three membrane-spanning regions. The amino-terminal 19 residues as well as a small loop in the 155 to 170 residue region appear exposed in the periplasm, while the carboxy terminus and a large loop after the first transmembrane region are cytoplasmic. Amino-terminal sequence analysis of TolQ purified from the membrane revealed the presence of the initiating formyl methionine group, suggesting a rapid translocation of the amino-terminal region across the cytoplasmic membrane. Analysis of various tolQ mutant strains suggests that the third transmembrane region as well as parts of the large cytoplasmic loop are necessary for activity.
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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.