ArticleBiochemistry2009
The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complex.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- A Suite of Designed Protein Cages Using Machine Learning Algorithms and Protein Fragment-Based Protocols.bioRxiv : the preprint server for biology · 2023Article
- The Cellular Abundance of Chemoreceptors, Chemosensory Signaling Proteins, Sensor Histidine Kinases, and Solute Binding Proteins ofInternational journal of molecular sciences · 2023Article
- Performance of halotolerant bacteria associated with Sahara-inhabiting halophytes Atriplex halimus L. and Lygeum spartum L. ameliorate tomato plant growth and tolerance to saline stress: from selective isolation to genomic analysis of potential determinants.World journal of microbiology & biotechnology · 2021Article
- Alternative Architecture of theBiomolecules · 2021Article
- ThemSystems · 2021Article
- The chemosensory systems of Vibrio cholerae.Molecular microbiology · 2020Review
- ATP Binding as a Key Target for Control of the Chemotaxis Kinase.Journal of bacteriology · 2020Article
- Type 1 Fimbriae and Motility Play a Pivotal Role During Interactions of Salmonella typhimurium with Acanthamoeba castellanii (T4 Genotype).Current microbiology · 2020Article
- Dynamics and clustering of IRE1α during ER stress.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations.Communications biology · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- New Twists and Turns in Bacterial Locomotion and Signal Transduction.Journal of bacteriology · 2019Review
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- Baseplate variability ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA.Journal of bacteriology · 2018Article
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- Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.Protein science : a publication of the Protein Society · 2017Article
- Cooperation of two distinct coupling proteins creates chemosensory network connections.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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2 authors.
Funding
Abstract
The chemosensory pathway of bacterial chemotaxis forms a polar signaling cluster in which the fundamental signaling units, the ternary complexes, are arrayed in a highly cooperative, repeating lattice. The repeating ternary units are composed of transmembrane receptors, histidine-kinase CheA, and coupling protein CheW, but it is unknown how these three core proteins are interwoven in the assembled ultrasensitive lattice. Here, to further probe the nature of the lattice, we investigate its stability. The findings reveal that once the signaling cluster is assembled, CheA remains associated and active for days in vitro. All three core components are required for this ultrastable CheA binding and for receptor-controlled kinase activity. The stability is disrupted by low ionic strength or high pH, providing strong evidence that electrostatic repulsion between the highly acidic core components can lead to disassembly. We propose that ultrastability arises from the assembled lattice structure that establishes multiple linkages between the core components, thereby conferring thermodynamic or kinetic ultrastability to the bound state. An important, known function of the lattice structure is to facilitate receptor cooperativity, which in turn enhances pathway sensitivity. In the cell, however, the ultrastability of the lattice could lead to uncontrolled growth of the signaling complex until it fills the inner membrane. We hypothesize that such uncontrolled growth is prevented by an unidentified intracellular disassembly system that is lost when complexes are isolated from cells, thereby unmasking the intrinsic complex ultrastability. Possible biological functions of ultrastability are discussed.
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