Disease relevance of cheR

• It has previously been reported that the alpha-proteobacterium Azospirillum brasilense undergoes methylation-independent chemotaxis; however, a recent study revealed cheB and cheR genes in this organism [1].
• A membrane from Escherichia coli cheX mutants failed to accept the methyl-moiety when incubated with a cytoplasm of wild type bacteria [2].

High impact information on cheR

• Analyses of cheR and/or cheB mutants, defective in receptor methylation/demethylation, show that response sensitivity depends on the activity of CheB and the level of receptor modification [3].
• We have constructed cheB, cheR, and cheBR mutants of A. brasilense and determined that the CheB and CheR proteins under study significantly influence chemotaxis and aerotaxis but are not essential for these behaviors to occur [1].
• Altered expression patterns in the absence of Dam methylation were also found for the chemotaxis genes cheR (repressed by Dam) and STM3216 (activated by Dam) and for the Braun lipoprotein gene, lppB (activated by Dam) [4].
• Second, in comparison to the wild type, cheB and cheR mutants under steady-state conditions exhibited an altered swimming bias, whereas the cheBR mutant and the che operon mutant did not [1].
• In comparison to the wild type, the cheB, cheR, and cheBR mutants showed various altered patterns of methanol release upon exposure to attractants [1].

Chemical compound and disease context of cheR

• Studies on bacterial chemotaxis. VI. Effect of cheX mutation on the methylation of methyl-accepting chemotaxis protein of Escherichia coli [2].

Biological context of cheR

• Deletion of the entire che operon (delta che), as well as nonpolar disruptions of cheAY, cheW, and cheR, resulted in a smooth-swimming phenotype, whereas disruption of cheB resulted in a locked tumbly phenotype [5].

Associations of cheR with chemical compounds

• Thus the decreased methylation of MCP in cheX mutants, as detected by the methyl-labeling experiment, is not caused by an effect of cheX mutation on the production of MCP back-bone protein but by a defect in the device for methylation [2].

Regulatory relationships of cheR

• Thus, the presence of a cheX defect blocked the stimulus-elicited appearance of faster migrating forms of the tsr product; conversely, the presence of a cheB defect resulted in a pronounced shift toward these forms in the absence of a chemotactic stimulus [6].

Other interactions of cheR

• The behavioral defect produced by overproduction of the CheW protein does not require the presence of the cheR, cheB, or cheZ gene [7].

Analytical, diagnostic and therapeutic context of cheR

• However, analysis of sulfur labeled proteins from cheX mutants by two-dimensional gel electrophoresis showed that the proportion of non-esterified MCP increased in cheX mutants while the total amount of MCP was not seriously affected [2].

References