Disease relevance of fliY-2

• Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex [1].
• CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli [2].

High impact information on fliY-2

• Signal transduction underlying bacterial chemotaxis involves excitatory phosphorylation and feedback control through deamidation and methylation of sensory receptors [3].
• A point mutation that dissociates CheC from CheD impairs chemotaxis in vivo [3].
• In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor [1].
• The CheA histidine kinase initiates the signal transduction pathway of bacterial chemotaxis by autophosphorylating a conserved histidine on its phosphotransferase domain (P1) [4].
• Sensory adaptation in bacterial chemotaxis is mediated by covalent modifications of specific glutamate and glutamine residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins (MCPs) [5].

Biological context of fliY-2

• Identification of methylation sites in Thermotoga maritima chemotaxis receptors [6].
• In addition to the chemotaxis genes, the fragment also encodes a putative protein isoaspartyl methyltransferase and an open reading frame of unknown function [7].

Anatomical context of fliY-2

• Here we report the in vitro methylation of chemoreceptors from Thermotoga maritima, a hyperthermophile that has served as a useful source of chemotaxis proteins for structural analysis [6].

Associations of fliY-2 with chemical compounds

• Although interfaces mediating protein-protein interactions are thought to be under strong evolutionary constraints, binding of the chemotaxis histidine kinase CheA to its phosphorylation target CheY suggests otherwise [8].
• Adaptation in bacterial chemotaxis involves reversible methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins [6].

References