ArticleJournal of bacteriology2005
Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Review
- A Two-Protein Chemoreceptor Complex Regulates Oxygen Thresholds in Bacterial Magneto-Aerotaxis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- 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
- Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.Journal of molecular biology · 2013Article
- 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
- Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptors.Journal of bacteriology · 2009Article
- Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.Journal of bacteriology · 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
- Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis.Molecular microbiology · 2006Article
- Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli.Journal of bacteriology · 2006Article
- Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer.Journal of bacteriology · 2006Article
- The Helicobacter pylori chemotaxis receptor TlpB (HP0103) is required for pH taxis and for colonization of the gastric mucosa.Journal of bacteriology · 2006Article
- Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer.Journal of bacteriology · 2006Article
- Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli.Journal of bacteriology · 2006Article
- Minimal requirements for oxygen sensing by the aerotaxis receptor Aer.Molecular microbiology · 2006Article
- The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding.Journal of bacteriology · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
HAMP domains are signal transduction domains typically located between the membrane anchor and cytoplasmic signaling domain of the proteins in which they occur. The prototypical structure consists of two helical amphipathic sequences (AS-1 and AS-2) connected by a region of undetermined structure. The Escherichia coli aerotaxis receptor, Aer, has a HAMP domain and a PAS domain with a flavin adenine dinucleotide (FAD) cofactor that senses the intracellular energy level. Previous studies reported mutations in the HAMP domain that abolished FAD binding to the PAS domain. In this study, using random and site-directed mutagenesis, we identified the distal helix, AS-2, as the component of the HAMP domain that stabilizes FAD binding. AS-2 in Aer is not amphipathic and is predicted to be buried. Mutations in the sequence coding for the contiguous proximal signaling domain altered signaling by Aer but did not affect FAD binding. The V264M residue replacement in this region resulted in an inverted response in which E. coli cells expressing the mutant Aer protein were repelled by oxygen. Bioinformatics analysis of aligned HAMP domains indicated that the proximal signaling domain is conserved in other HAMP domains that are not involved in chemotaxis or aerotaxis. Only one null mutation was found in the coding sequence for the HAMP AS-1 and connector regions, suggesting that these are not active signal transduction sites. We consider a model in which the signal from FAD is transmitted across a PAS-HAMP interface to AS-2 or the proximal signaling domain.
Indexed as
Identifiers
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.