ArticleJournal of bacteriology2000
Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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
23 citing papers in PubMed, 63 citations in OpenAlex.
- Review
- The role of TolA, TolB, and TolR in cell morphology, OMVs production, and virulence of Salmonella Choleraesuis.AMB Express · 2022Article
- Subunit vaccines forFrontiers in immunology · 2022Review
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli.PLoS genetics · 2017Article
- Thermotolerant genes essential for survival at a critical high temperature in thermotolerant ethanologenicBiotechnology for biofuels · 2017Article
- Localization of the outer membrane protein OmpA2 in Caulobacter crescentus depends on the position of the gene in the chromosome.Journal of bacteriology · 2014Article
- Polar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complex.Molecular microbiology · 2014Article
- Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Virulence determinants, drug resistance and mobile genetic elements of Laribacter hongkongensis: a genome-wide analysis.Cell & bioscience · 2011Article
- The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor.Journal of bacteriology · 2010Article
- Protein docking by Rotation-Based Uniform Sampling (RotBUS) with fast computing of intermolecular contact distance and residue desolvation.BMC bioinformatics · 2010Article
- Genome-wide screens: novel mechanisms in colicin import and cytotoxicity.Molecular microbiology · 2009Article
- Protein disorder is positively correlated with gene expression in Escherichia coli.Journal of proteome research · 2008Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli.Molecular microbiology · 2007Article
- Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane.Journal of bacteriology · 2003Article
- Identification and genetic characterization of PmrA-regulated genes and genes involved in polymyxin B resistance in Salmonella enterica serovar typhimurium.Infection and immunity · 2002Article
- 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Tol-Pal system of Escherichia coli is involved in maintaining outer membrane stability. Mutations in tolQ, tolR, tolA, tolB, or pal genes result in sensitivity to bile salts and the leakage of periplasmic proteins. Moreover, some of the tol genes are necessary for the entry of group A colicins and the DNA of filamentous bacteriophages. TolQ, TolR, and TolA are located in the cytoplasmic membrane where they interact with each other via their transmembrane domains. TolB and Pal form a periplasmic complex near the outer membrane. We used suppressor genetics to identify the regions important for the interaction between TolB and Pal. Intragenic suppressor mutations were characterized in a domain of Pal that was shown to be involved in interactions with TolB and peptidoglycan. Extragenic suppressor mutations were located in tolB gene. The C-terminal region of TolB predicted to adopt a beta-propeller structure was shown to be responsible for the interaction of the protein with Pal. Unexpectedly, none of the suppressor mutations was able to restore a correct association between Pal and peptidoglycan, suggesting that interactions between Pal and other components such as TolB may also be important for outer membrane stability.
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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.