ArticleJournal of bacteriology2006
Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 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.
The trial behind it
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
16 citing papers in PubMed, 25 citations in OpenAlex.
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- Review
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- The Aer2 receptor from Vibrio cholerae is a dual PAS-heme oxygen sensor.Molecular microbiology · 2018Article
- Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer.Molecular microbiology · 2016Article
- Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Charting the signal trajectory in a light-oxygen-voltage photoreceptor by random mutagenesis and covariance analysis.The Journal of biological chemistry · 2013Article
- Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.Journal of molecular biology · 2013Article
- PAS domain residues and prosthetic group involved in BdlA-dependent dispersion response by Pseudomonas aeruginosa biofilms.Journal of bacteriology · 2012Article
- Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.Journal of bacteriology · 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
- Myxococcus xanthus Pph2 is a manganese-dependent protein phosphatase involved in energy metabolism.The Journal of biological chemistry · 2009Article
- Changes in quaternary structure in the signaling mechanisms of PAS domains.Biochemistry · 2008Article
- Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.Journal of bacteriology · 2008Article
- Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy.Molecular microbiology · 2007Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Aer, the Escherichia coli receptor for behavioral responses to oxygen (aerotaxis), energy, and redox potential, contains a PAS sensory-input domain. Within the PAS superfamily, the N-terminal segment (N-cap) is poorly conserved and its role is not well understood. We investigated the role of the N-cap (residues 1 to 19) in the Aer PAS domain by missense and truncation mutagenesis. Aer-PAS N-cap truncations and an Aer-M21P substitution resulted in low cellular levels of the mutant proteins, suggesting that the N-terminal region was important for stabilizing the structure of the PAS domain. The junction of the N-cap and PAS core was critical for signaling in Aer. Mutations and truncations in the sequence encoding residues 15 to 21 introduced a range of phenotypes, including defects in FAD binding, constant tumbling motility, and an inverse response in which E. coli cells migrated away from oxygen concentrations to which they are normally attracted. The proximity of two N-cap regions in an Aer dimer was assessed in vivo by oxidatively cross-linking serial cysteine substitutions. Cross-linking of several cysteine replacements at 23 degrees C was attenuated at 10 degrees C, indicating contact was not at a stable dimer interface but required lateral mobility. We observed large multimers of Aer when we combined cross-linking of N-cap residues with a cysteine replacement that cross-links exclusively at the Aer dimer interface. This suggests that the PAS N-cap faces outwards in a dimer and that PAS-PAS contacts can occur between adjacent dimers.
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What OpenQuestion holds
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.