The N-terminal cytoplasmic tail of the aspartate receptor is not essential in signal transduction of bacterial chemotaxis.
To determine the role in transmembrane signaling of the N-terminal peptide of the first transmembrane region of the aspartate receptor, it was subjected to extensive mutagenesis. Drastic changes did not alter the chemotactic ability of the receptor to aspartate significantly. Thus the cytoplasmic N terminus of the first transmembrane region does not play an essential role in transmembrane signaling, and the entire signal that is transmitted to the cytoplasmic domain must be sent through the second transmembrane region. This eliminates the models requiring an interaction of this N-terminal peptide with the remaining cytoplasmic portion of the receptor.
Chen
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Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
Koshland
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D001224:Aspartic Acid / Q000378:metabolism; D002462:Cell Membrane / Q000502:physiology; D002633:Chemotaxis; D003593:Cytoplasm / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D007700:Kinetics; D016296:Mutagenesis; D010957:Plasmids; D017459:Receptors, Amino Acid / Q000096:biosynthesis / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D017384:Sequence Deletion; D015398:Signal Transduction
D017459:Receptors, Amino Acid; D011994:Recombinant Proteins; C031959:aspartic acid receptor; D001224:Aspartic Acid