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Science 3 June 1983:
Vol. 220. no. 4601, pp. 1016 - 1020
DOI: 10.1126/science.6302843
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Articles

Science, Vol 220, Issue 4601, 1016-1020
Copyright © 1983 by American Association for the Advancement of Science

articles

Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing

AF Russo and DE Koshland Jr

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.


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A Model for Transmembrane Signaling in a Bacterial Chemotaxis Receptor.
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Structure-Function Studies of Bacterial Chemosensors.
P. Ames, J. Chen, C. Wolff, and J.S. Parkinson (1988)
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Global flexibility in a sensory receptor: a site-directed cross-linking approach.
J. Falke and D. Koshland Jr (1987)
Science 237, 1596-1600
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Transmission of Regulatory Conformational Changes through Proteins.
P.E. Thorsness, S.L. Mowbray, and D.E. Koshland Jr. (1987)
Cold Spring Harb Symp Quant Biol 52, 623-630
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A genetic approach to analyzing membrane protein topology.
C Manoil and J Beckwith (1986)
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Bacterial Chemotaxis and Molecular Neurobiology.
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Mutations That Affect Ligand Binding to the Escherichia coli Aspartate Receptor. IMPLICATIONS FOR TRANSMEMBRANE SIGNALING.
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