ArticleJournal of bacteriology2003
Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 83 citations in OpenAlex.
- Regulation of Resistance in Vancomycin-Resistant Enterococci: The VanRS Two-Component System.Microorganisms · 2021Review
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis.PLoS pathogens · 2020Article
- EnvZ/OmpR Two-Component Signaling: An Archetype System That Can Function Noncanonically.EcoSal Plus · 2020Review
- Hybrid Two-Component Sensors for Identification of Bacterial Chemoreceptor Function.Applied and environmental microbiology · 2019Article
- Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.Biophysical journal · 2017Article
- Novel Two-Step Hierarchical Screening of Mutant Pools Reveals Mutants under Selection in Chicks.Infection and immunity · 2016Article
- Signal transduction in histidine kinases: insights from new structures.Structure (London, England : 1993) · 2015Review
- HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors.PLoS biology · 2013Article
- HAMP domain-mediated signal transduction probed with a mycobacterial adenylyl cyclase as a reporter.The Journal of biological chemistry · 2012Article
- Differential control of Yersinia pestis biofilm formation in vitro and in the flea vector by two c-di-GMP diguanylate cyclases.PloS one · 2011Article
- Interactions among HAMP domain repeats act as an osmosensing molecular switch in group III hybrid histidine kinases from fungi.The Journal of biological chemistry · 2010Article
- Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.Current opinion in microbiology · 2010Review
- Use of two-component signal transduction systems in the construction of synthetic genetic networks.Current opinion in microbiology · 2010Review
- Structure of concatenated HAMP domains provides a mechanism for signal transduction.Structure (London, England : 1993) · 2010Article
- The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Journal of bacteriology · 2010Article
- Transmembrane signaling in chimeras of the Escherichia coli aspartate and serine chemotaxis receptors and bacterial class III adenylyl cyclases.The Journal of biological chemistry · 2010Article
- LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structural analysis of ligand stimulation of the histidine kinase NarX.Structure (London, England : 1993) · 2009Article
- Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptors.Journal of bacteriology · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The HAMP linker, a predicted structural element observed in many sensor kinases and methyl-accepting chemotaxis proteins, transmits signals between sensory input modules and output modules. HAMP linkers are located immediately inside the cytoplasmic membrane and are predicted to form two short amphipathic alpha-helices (AS-1 and AS-2) joined by an unstructured connector. HAMP linkers are found in the Escherichia coli nitrate- and nitrite-responsive sensor kinases NarX and NarQ (which respond to ligand by increasing kinase activity) and the sensor kinase CpxA (which responds to ligand by decreasing kinase activity). We constructed a series of hybrids with fusion points throughout the HAMP linker, in which the sensory modules of NarX or NarQ are fused to the transmitter modules of NarX, NarQ, or CpxA. A hybrid of the NarX sensor module and the CpxA HAMP linker and transmitter module (NarX-CpxA-1) responded to nitrate by decreasing kinase activity, whereas a hybrid in which the HAMP linker of NarX was replaced by that of CpxA (NarX-CpxA-NarX-1) responded to nitrate by increasing kinase activity. However, sequence variations between HAMP linkers do not allow free exchange of HAMP linkers or their components. Certain deletions in the NarX HAMP linker resulted in characteristic abnormal responses to ligand; similar deletions in the NarQ and NarX-CpxA-1 HAMP linkers resulted in responses to ligand generally similar to those seen in NarX. We conclude that the structure and action of the HAMP linker are conserved and that the HAMP linker transmits a signal to the output domain that ligand is bound.
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