Disease relevance of cheY

• Characterization of the cheY genes from Leptospira interrogans and their effects on the behavior of Escherichia coli [1].
• The thermal stability of the bacterial chemotaxis protein CheY from Salmonella typhimurium has been examined by thermal denaturation at pH 7.0 in the presence of guanidine-HCl and urea [2].

High impact information on cheY

• Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY [3].
• We found that chemotaxis in the cheW Che+ suppressor depended on both cheY and cheA [4].
• Exogenous fumarate, in the intracellular presence of the chemotaxis protein CheY, restored switching ability to envelopes, with a concomitant increase in clockwise rotation [5].
• The cheY suppressor mutations which have previously been mapped to flaB were further localized to flaB11 (Parkinson et al., J. Bacteriol. 155:265-274, 1983) [6].

Biological context of cheY

• These are the first examples of cheY mutations that reduce sensitivity to the phosphatase activity of CheZ without being altered in terms of their intrinsic phosphorylation and autodephosphorylation rates [7].

Analytical, diagnostic and therapeutic context of cheY

• Reverse-transcriptase-polymerase chain reaction (RT-PCR) data indicated that cheA through cheY are co-transcribed and suggested that transcription is terminated after cheY [8].
• Northern blot and primer extension analysis suggested that cheY and cheA are transcribed as a bicistronic unit and that the transcription is thermoregulated [9].

References