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Science 13 December 1991:
Vol. 254. no. 5038, pp. 1651 - 1654
DOI: 10.1126/science.1661030
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Articles

Science, Vol 254, Issue 5038, 1651-1654
Copyright © 1991 by American Association for the Advancement of Science

articles

Intrasubunit signal transduction by the aspartate chemoreceptor

DL Milligan and DE Koshland Jr

Department of Molecular and Cell Biology, University of California, Berkeley 94720.

Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.


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