ArticleJournal of bacteriology2004
Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 40 citations in OpenAlex.
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- Review
- Sensing the Reducing Power to Determine the Cell Fate: Flavin Redox-Switches in Signal Transduction.Current microbiology · 2025Review
- A PilZ-Containing Chemotaxis Receptor Mediates Oxygen and Wheat Root Sensing inFrontiers in microbiology · 2019Article
- A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea.Cellular and molecular life sciences : CMLS · 2017Review
- Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer.Molecular microbiology · 2016Article
- Article
- Identification and characterization of three Vibrio alginolyticus non-coding RNAs involved in adhesion, chemotaxis, and motility processes.Frontiers in cellular and infection microbiology · 2015Article
- Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.Journal of molecular biology · 2013Article
- Salmonella chemoreceptors McpB and McpC mediate a repellent response to L-cystine: a potential mechanism to avoid oxidative conditions.Molecular microbiology · 2012Article
- Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.Journal of bacteriology · 2011Article
- PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor.Molecular microbiology · 2011Article
- Role of the F1 region in the Escherichia coli aerotaxis receptor Aer.Journal of bacteriology · 2011Article
- Gain-of-function mutations cluster in distinct regions associated with the signalling pathway in the PAS domain of the aerotaxis receptor, Aer.Molecular microbiology · 2010Article
- Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni.Molecular microbiology · 2008Article
- Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.Journal of bacteriology · 2008Article
- Organization of the aerotaxis receptor aer in the membrane of Escherichia coli.Journal of bacteriology · 2007Article
- Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy.Molecular microbiology · 2007Review
- Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer.Journal of bacteriology · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli energy-sensing Aer protein initiates aerotaxis towards environments supporting optimal cellular energy. The Aer sensor is an N-terminal, FAD-binding, PAS domain. The PAS domain is linked by an F1 region to a membrane anchor, and in the C-terminal half of Aer, a HAMP domain links the membrane anchor to the signaling domain. The F1 region, membrane anchor, and HAMP domain are required for FAD binding. Presumably, alterations in the redox potential of FAD induce conformational changes in the PAS domain that are transmitted to the HAMP and C-terminal signaling domains. In this study we used random mutagenesis and intragenic pseudoreversion analysis to examine functional interactions between the HAMP domain and the N-terminal half of Aer. Missense mutations in the HAMP domain clustered in the AS-2 alpha-helix and abolished FAD binding to Aer, as previously reported. Three amino acid replacements in the Aer-PAS domain, S28G, A65V, and A99V, restored FAD binding and aerotaxis to the HAMP mutants. These suppressors are predicted to surround a cleft in the PAS domain that may bind FAD. On the other hand, suppression of an Aer-C253R HAMP mutant was specific to an N34D substitution with a predicted location on the PAS surface, suggesting that residues C253 and N34 interact or are in close proximity. No suppressor mutations were identified in the F1 region or membrane anchor. We propose that functional interactions between the PAS domain and the HAMP AS-2 helix are required for FAD binding and aerotactic signaling by Aer.
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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.