MicroReview: Functional similarities among two‐component sensors and methyl‐accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction

Williams, Stanly B.; Stewart, Valley

doi:10.1046/j.1365-2958.1999.01562.x

Cited by 129 publications

(128 citation statements)

References 53 publications

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“…In this way, the HAMP domain serves as a linker region that is suggested to be conserved in histidine kinases, adenylyl cyclases, methylaccepting chemotaxis proteins and phosphatases, and converts ligand-induced conformational changes into kinase-controlling signals (Aravind & Ponting, 1999;Butler & Falke, 1998;Le Moual & Koshland, 1996;Williams & Stewart, 1999). Cj0951c shows strong homologies to the cytoplasmic signalling domains of MCPs, being composed of an adaptation region with methylation sites, a flexible region with a conserved glycine hinge, and a protein-interaction region for binding of the chemotaxis protein CheW and the kinase CheA (Hazelbauer et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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Campylobacter jejuni, an important food-borne bacterial pathogen in industrialized countries and in the developing world, is one of the major causes of bacterial diarrhoea. To identify genes which are important for the invasion of host cells by the pathogen, we screened altogether 660 clones of a transposon-generated mutant library based on the clinical C. jejuni isolate B2. Thereby, we identified a clone with a transposon insertion in gene cj0952c. As in the well-characterized C. jejuni strain NCTC 11168, the corresponding protein together with the gene product of the adjacent gene cj0951c consists of two transmembrane domains, a HAMP domain and a putative MCP domain, which together are thought to act as a chemoreceptor, designated Tlp7. In this report we show that genes cj0952c and cj0951c (i) are important for the host cell invasion of the pathogen, (ii) are not translated as one protein in C. jejuni isolate B2, contradicting the idea of a postulated read-through mechanism, (iii) affect the motility of C. jejuni, (iv) alter the chemotactic behaviour of the pathogen towards formic acid, and (v) are not related to the utilization of formic acid by formate dehydrogenase.

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Section: Discussionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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“…Sequence conservation is more subtle among HAMP modules [42,45] but 3D structure is probably shared for the approximately two-thirds of all chemoreceptors that contain the module [43]. There is substantial variation in the sequence and in the deduced 3D organization among transmembrane sensing modules, but the antiparallel four-helix bundle seems to be the most common structure [65] and this structure can be conserved even with minimal sequence identity [66].…”

Section: Box 3 Functional Architecture Of the Chemoreceptor Dimermentioning

confidence: 99%

“…A recent advance comes from nuclear magnetic resonance (NMR) characterization of an isolated HAMP domain from an archaeal, hyperthermophilic, transmembrane protein of unknown function [43] (Box 3). HAMP domains, characterized by two amphiphilic helices joined by a linker [44], occur in many bacterial signaling proteins [42,45]. Typically, HAMP domains are located between transmembrane and cytoplasmic signaling regions of known or putative transmembrane receptors, consistent with a role in converting ligand-induced conformational changes into kinase-controlling signals.…”

Section: Chemoreceptor Homodimers: Structurementioning

confidence: 99%

Bacterial chemoreceptors: high-performance signaling in networked arrays

Hazelbauer

Falke

Parkinson

2008

Trends in Biochemical Sciences

588

804

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Chemoreceptors are crucial components in the bacterial sensory systems that mediate chemotaxis. Chemotactic responses exhibit exquisite sensitivity, extensive dynamic range and precise adaptation. The mechanisms that mediate these high-performance functions involve not only actions of individual proteins but also interactions among clusters of components, localized in extensive patches of thousands of molecules. Recently, these patches have been imaged in native cells, important features of chemoreceptor structure and on-off switching have been identified, and new insights have been gained into the structural basis and functional consequences of higher order interactions among sensory components. These new data suggest multiple levels of molecular interactions, each of which contribute specific functional features and together create a sophisticated signaling device. High-performance signaling in bacterial chemotaxisThe high-performance chemotaxis signaling system of Escherichia coli (Box 1) involves a limited number of components but notable sophistication [1][2][3][4]. This system has become a paradigm for molecular characterization of biological signaling mechanisms. Transmembrane chemoreceptors, known as methyl-accepting chemotaxis proteins (MCPs), direct cell locomotion by regulating the histidine kinase CheA; CheA phosphorylates a response regulator, which in turn controls the rotational direction of the flagellar motor. Chemotactic sensitivity and the range of signal detection are regulated by adaptational modification of chemoreceptors via reversible glutamyl methylation. The resulting interplay between motor control and sensory adaptation produces directed motile behavior. E. coli chemoreceptors are the most extensively studied representatives of the MCP super-family, central components of homologous systems that mediate tactic responses [5,6] across the phylogenetic diversity of bacteria and archaea [7].In E. coli chemotaxis proteins cluster in membrane-associated patches [8]. Interaction within patches is thought to contribute to notable features of the signaling system: high sensitivity, wide dynamic range, extensive cooperativity and precise adaptation. Delineating the molecular mechanisms underlying these features will require knowledge of structures of the components, complexes and higher order arrays. In addition it will require definition of organization at the multiple levels of interaction among signaling components and an understanding of the changes in components and their interactions that mediate signaling at each level. In the past few years, notable progress has been made toward acquiring the NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript information and insights necessary for understanding these molecular mechanisms. This review describes that progress. Here we follow the lead of most investigators in the area, and do not distinguish between studies of first cousins E. coli and Salmonella enterica serovar Typhimurium. Thus, referenc...

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“…This prototypic domain organization can be varied by inclusion of "linker" regions, such as the HAMP or PAS domain (12,276), between TMR2 and the transmitter domain or by additional phosphorylation domains downstream of the transmitter domain (Fig. 2).…”

Section: Periplasmic-sensing Histidine Kinasesmentioning

confidence: 99%

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Mascher

Helmann

Unden

2006

Microbiol Mol Biol Rev

624

652

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SUMMARY Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sensing. In order to gain insight into the mechanisms of stimulus perception by bacterial histidine kinases, we here survey sensor domain architecture and topology within the bacterial membrane, functional aspects related to this topology, and sequence and phylogenetic conservation. Based on these criteria, three groups of histidine kinases can be differentiated. (i) Periplasmic-sensing histidine kinases detect their stimuli (often small solutes) through an extracellular input domain. (ii) Histidine kinases with sensing mechanisms linked to the transmembrane regions detect stimuli (usually membrane-associated stimuli, such as ionic strength, osmolarity, turgor, or functional state of the cell envelope) via their membrane-spanning segments and sometimes via additional short extracellular loops. (iii) Cytoplasmic-sensing histidine kinases (either membrane anchored or soluble) detect cellular or diffusible signals reporting the metabolic or developmental state of the cell. This review provides an overview of mechanisms of stimulus perception for members of all three groups of bacterial signal-transducing histidine kinases.

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MicroReview: Functional similarities among two‐component sensors and methyl‐accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction

Cited by 129 publications

References 53 publications

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Bacterial chemoreceptors: high-performance signaling in networked arrays

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

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