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Science 18 October 1996:
Vol. 274. no. 5286, pp. 425 - 426
DOI: 10.1126/science.274.5286.425
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Reports
Attractant Signaling by an Aspartate Chemoreceptor Dimer with a
Single Cytoplasmic Domain
Paul J. Gardina
and
Michael D. Manson
*
Signal transduction across cell membranes often involves
interactions among identical receptor subunits, but the contribution of
individual subunits is not well understood. The chemoreceptors of
enteric bacteria mediate attractant responses by interrupting a
phosphotransfer circuit initiated at receptor complexes with the
protein kinase CheA. The aspartate receptor (Tar) is a
homodimer, and oligomerized cytoplasmic domains stimulate CheA activity
much more than monomers do in vitro. Intragenic complementation was
used to show in Escherichia coli that heterodimers
containing one full-length and one truncated Tar subunit mediated
responses to aspartate in the presence of full-length Tar homodimers
that could not bind aspartate. Thus, a Tar dimer containing only one
cytoplasmic domain can initiate an attractant (inhibitory) signal,
although it may not be able to stimulate kinase activity of CheA.
Department of Biology, Texas A&M University, College Station, TX
77840, USA.
*
To whom correspondence should be addressed.
Read the Full Text
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