Stabilization of Polar Localization of a Chemoreceptor via Its Covalent Modifications and Its Communication with a Different Chemoreceptor

• DOI: 10.1128/jb.187.22.7647-7654.2005
• Publication Date: 2005-11-02T22:07:52Z
• Authors: Daisuke Shiomi; Satomi Banno; Michio Homma; Ikuro Kawagishi
• Keywords: 0301 basic medicine; Histidine Kinase; Escherichia coli Proteins; Recombinant Fusion Proteins; Green Fluorescent Proteins; Cell Polarity; Membrane Proteins; Methyl-Accepting Chemotaxis Proteins; Receptors, Cell Surface; Methylation; Chemoreceptor Cells; 03 medical and health sciences; Bacterial Proteins; Microscopy, Fluorescence; Genes, Reporter; Escherichia coli

In the chemotaxis of Escherichia coli, polar clustering chemoreceptors, histidine kinase CheA, and adaptor protein CheW is thought to be involved in signal amplification adaptation. However, mechanism that leads localization receptor still largely unknown. this study, we examined effect covalent modification on aspartate chemoreceptor Tar fused green fluorescent (GFP). Amidation (and presumably methylation) Tar-GFP enhanced its own localization, although was small. The slight but significant amidation reinforced by fact a noncatalytic mutant version GFP-CheR targets C-terminal pentapeptide sequence similarly facilitated amidation. Polar demethylated also increasing levels serine Tsr. itself may too small account for chemotactic adaptation, suggested contribute molecular assembly chemoreceptor/histidine array at cell pole, stabilizing dimer-to-dimer interaction.