Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing.
In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D001224:Aspartic Acid; D018407:Bacterial Physiological Phenomena; D001483:Base Sequence; D002633:Chemotaxis; D004926:Escherichia coli / Q000502:physiology; D008745:Methylation; D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface / Q000235:genetics / Q000502:physiology*; D012486:Salmonella typhimurium / Q000502:physiology; D012694:Serine
D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface; C031959:aspartic acid receptor; C038039:serine receptor; D001224:Aspartic Acid; D012694:Serine