ArticleProceedings of the National Academy of Sciences of the United States of America2010
Signal-dependent turnover of the bacterial flagellar switch protein FliM.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 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
97 citing papers in PubMed.
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- PrtA-mediated flagellar turnover is essential for robust biofilm development inApplied and environmental microbiology · 2025Article
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- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- MaxCal can infer models from coupled stochastic trajectories of gene expression and cell division.Biophysical journal · 2023Article
- GFP fusions of Sec-routed extracellular proteins inMicrobial cell (Graz, Austria) · 2023Article
- Structure and Assembly of theInternational journal of molecular sciences · 2023Article
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- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Modeling Non-additive Effects in Neighboring Chemically Identical Fluorophores.The journal of physical chemistry. B · 2022Article
- The Effect of the Second Messenger c-di-GMP on Bacterial Chemotaxis in Escherichia coli.Applied and environmental microbiology · 2022Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacterial Proprioception: Can a Bacterium Sense Its Movement?Frontiers in microbiology · 2022Review
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- Quantitative proteomic analysis provides insight into the survival mechanism ofCurrent research in food science · 2022Article
- Dynamics of Proteins and Macromolecular Machines in Escherichia coli.EcoSal Plus · 2021Review
37 more citing papers are in PubMed but not listed here.
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Abstract
Most biological processes are performed by multiprotein complexes. Traditionally described as static entities, evidence is now emerging that their components can be highly dynamic, exchanging constantly with cellular pools. The bacterial flagellar motor contains approximately 13 different proteins and provides an ideal system to study functional molecular complexes. It is powered by transmembrane ion flux through a ring of stator complexes that push on a central rotor. The Escherichia coli motor switches direction stochastically in response to binding of the response regulator CheY to the rotor switch component FliM. Much is known of the static motor structure, but we are just beginning to understand the dynamics of its individual components. Here we measure the stoichiometry and turnover of FliM in functioning flagellar motors, by using high-resolution fluorescence microscopy of E. coli expressing genomically encoded YPet derivatives of FliM at physiological levels. We show that the approximately 30 FliM molecules per motor exist in two discrete populations, one tightly associated with the motor and the other undergoing stochastic turnover. This turnover of FliM molecules depends on the presence of active CheY, suggesting a potential role in the process of motor switching. In many ways the bacterial flagellar motor is as an archetype macromolecular assembly, and our results may have further implications for the functional relevance of protein turnover in other large molecular complexes.
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