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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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Electron Microscopic Analysis of Membrane Assemblies Formed by the Bacterial Chemotaxis Receptor Tsr.
R. M. Weis, T. Hirai, A. Chalah, M. Kessel, P. J. Peters, and S. Subramaniam (2003)
J. Bacteriol. 185, 3636-3643
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Rotational On-off Switching of a Hybrid Membrane Sensor Kinase Tar-ArcB in Escherichia coli.
O. Kwon, D. Georgellis, and E. C. C. Lin (2003)
J. Biol. Chem. 278, 13192-13195
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Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity.
S.-H. Kim, W. Wang, and K. K. Kim (2002)
PNAS 99, 11611-11615
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A Piston Model for Transmembrane Signaling of the Aspartate Receptor.
K. M. Ottemann, W. Xiao, Y. Shin, and D. E. Koshland Jr. (1999)
Science 285, 1751-1754
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Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.
Y. Zhang, P. J. Gardina, A. S. Kuebler, H. S. Kang, J. A. Christopher, and M. D. Manson (1999)
PNAS 96, 939-944
   Abstract »    Full Text »    PDF »
Chemotactic Adaptation Is Altered by Changes in the Carboxy-Terminal Sequence Conserved among the Major Methyl-Accepting Chemoreceptors.
H. Okumura, S.-i. Nishiyama, A. Sasaki, M. Homma, and I. Kawagishi (1998)
J. Bacteriol. 180, 1862-1868
   Abstract »    Full Text »
Chimeric Chemoreceptors in Escherichia coli: Signaling Properties of Tar-Tap and Tap-Tar Hybrids.
S. Weerasuriya, B. M. Schneider, and M. D. Manson (1998)
J. Bacteriol. 180, 914-920
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Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain.
K. M. Ottemann and D. E. Koshland Jr. (1997)
PNAS 94, 11201-11204
   Abstract »    Full Text »    PDF »
The N-terminal Cytoplasmic Tail of the Aspartate Receptor Is Not Essential in Signal Transduction of Bacterial Chemotaxis.
X. Chen and D. E. Koshland , Jr. (1995)
J. Biol. Chem. 270, 24038-24042
   Abstract »    Full Text »    PDF »
Interactions between the Methylation Sites of the Escherichia coli Aspartate Receptor Mediated by the Methyltransferase.
M. J. Shapiro, D. Panomitros, and D. E. Koshland Jr. (1995)
J. Biol. Chem. 270, 751-755
   Abstract »    Full Text »    PDF »
Receptors and Transmembrane Signaling.
B.L. Stoddard, H.-P. Biemann, and D.E. Koshland Jr. (1992)
Cold Spring Harb Symp Quant Biol 57, 1-15
   Abstract »    PDF »
A Model for Transmembrane Signaling in a Bacterial Chemotaxis Receptor.
S.-H. Kim, G.G. Prive, J. Yeh, W.G. Scott, and M.V. Milburn (1992)
Cold Spring Harb Symp Quant Biol 57, 17-24
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Intrasubunit signal transduction by the aspartate chemoreceptor.
D. Milligan and D. Koshland Jr (1991)
Science 254, 1651-1654
   Abstract »    PDF »
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand.
M. Milburn, G. Prive, D. Milligan, W. Scott, J Yeh, J Jancarik, D. Koshland Jr, and S. Kim (1991)
Science 254, 1342-1347
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Bacterial Microprocessing.
H.C. Berg (1990)
Cold Spring Harb Symp Quant Biol 55, 539-545
   Abstract »    PDF »
A chemoattractant receptor controls development in Dictyostelium discoideum.
P. Klein, T. Sun, C. Saxe 3rd, A. Kimmel, R. Johnson, and P. Devreotes (1988)
Science 241, 1467-1472
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Nucleotide sequence and structure of the sevenless gene of Drosophila melanogaster..
D D Bowtell, M A Simon, and G M Rubin (1988)
Genes & Dev. 2, 620-634
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A Physicist Looks at Bacterial Chemotaxis.
H.C. Berg (1988)
Cold Spring Harb Symp Quant Biol 53, 1-9
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Roles of Methylation and Phosphorylation in the Bacterial Sensing System.
D.E. Koshland Jr., D.A. Sanders, and R.M. Weis (1988)
Cold Spring Harb Symp Quant Biol 53, 11-17
   Abstract »    PDF »
Structure-Function Studies of Bacterial Chemosensors.
P. Ames, J. Chen, C. Wolff, and J.S. Parkinson (1988)
Cold Spring Harb Symp Quant Biol 53, 59-65
   Abstract »    PDF »
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
J. Falke and D. Koshland Jr (1987)
Science 237, 1596-1600
   Abstract »    PDF »
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)
Science 233, 1403-1408
   Abstract »    PDF »
Bacterial Chemotaxis and Molecular Neurobiology.
J. Adler (1983)
Cold Spring Harb Symp Quant Biol 48, 803-804
   Abstract »    PDF »
Information Processing in a Sensory System.
D.E. Koshland Jr., A.F. Russo, and N.I. Gutterson (1983)
Cold Spring Harb Symp Quant Biol 48, 805-810
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Mutations That Affect Ligand Binding to the Escherichia coli Aspartate Receptor. IMPLICATIONS FOR TRANSMEMBRANE SIGNALING.
A. M. Bjorkman, P. Dunten, M. O. J. Sandgren, V. N. Dwarakanath, and S. L. Mowbray (2001)
J. Biol. Chem. 276, 2808-2815
   Abstract »    Full Text »    PDF »


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