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Science 10 September 1999:
Vol. 285. no. 5434, pp. 1751 - 1754
DOI: 10.1126/science.285.5434.1751
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Reports

A Piston Model for Transmembrane Signaling of the Aspartate Receptor

Karen M. Ottemann, 1*dagger Wenzhong Xiao, 2* Yeon-Kyun Shin, 2ddagger Daniel E. Koshland Jr. 1ddagger

To characterize the mechanism by which receptors propagate conformational changes across membranes, nitroxide spin labels were attached at strategic positions in the bacterial aspartate receptor. By collecting the electron paramagnetic resonance spectra of these labeled receptors in the presence and absence of the ligand aspartate, ligand binding was shown to generate an ~1 angstrom intrasubunit piston-type movement of one transmembrane helix downward relative to the other transmembrane helix. The receptor-associated phosphorylation cascade proteins CheA and CheW did not alter the ligand-induced movement. Because the piston movement is very small, the ability of receptors to produce large outcomes in response to stimuli is caused by the ability of the receptor-coupled enzymes to detect small changes in the conformation of the receptor.

1 Department of Molecular and Cell Biology and
2 Department of Chemistry, University of California, Berkeley, CA 94720, USA.
*   These authors contributed equally to this work.

dagger    Present address: Departments of Biology and Environmental Toxicology, University of California at Santa Cruz, CA 95064, USA.

ddagger    To whom correspondence should be addressed. E-mail: shin{at}cchem.berkeley.edu (Y.-K.S.); dek{at}uclink4.berkeley.edu (D.E.K).

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