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POSTERS - BLAST X - University of Utah

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<strong>BLAST</strong> X Thurs. Evening Session<br />

MINOR RECEPTOR SIGNALLING IN E. COLI<br />

Silke Neumann, Ned Wingreen* and Victor Sourjik<br />

Ruprecht-Karls-Universität Heidelberg, Zentrum für molekulare Biologie Heidelberg (ZMBH), Im<br />

Neuenheimer Feld 282, 69120 Heidelberg, Germany<br />

* Department <strong>of</strong> Molecular Biology - Princeton <strong>University</strong><br />

Ligand recognition in the chemotaxis pathway <strong>of</strong> E. coli proceeds through binding <strong>of</strong><br />

ligands to transmembrane receptors, either directly or indirectly through periplasmic binding<br />

proteins. E. coli has five types <strong>of</strong> receptors, with two high-abundance (or major) receptors – Tsr<br />

for serine and Tar for aspartate and maltose – and three low-abundance (or minor) receptors –<br />

Tap for dipeptides, Trg for ribose, galactose and glucose, and Aer for redox potential. Together<br />

with the histidine kinase CheA, receptors form chemosensory complexes which in turn are<br />

organized in tight clusters where receptors <strong>of</strong> different ligand specificities are intermixed. Signal<br />

processing is thought to occur within these receptor clusters through allosteric interactions<br />

between receptor dimers. To compare signal processing by minor and major receptors, we<br />

systematically investigated responses mediated by Trg and Tap, and by Tar and Tsr in respect<br />

to response sensitivity, relation between receptor occupancy and kinase inactivation, dynamic<br />

range <strong>of</strong> the response, adaptation time to a range <strong>of</strong> stimuli, as well as integration <strong>of</strong> signals that<br />

are sensed by different receptors using an in vivo FRET-based kinase assay. Our experimental<br />

analysis shows that signals are amplified and integrated differently by the two receptor<br />

populations, but in both cases signal processing can be quantitatively explained by the same<br />

allosteric model.<br />

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