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Biophys J, April 2002, p. 1809-1817, Vol. 82, No. 4
Department of Zoology, University of Cambridge, Cambridge CB2 3EJ, United Kingdom
Adaptation of the attractant response in
Escherichia coli is attributable to the methylation of
its transmembrane chemotactic receptors by the methyltransferase CheR.
This protein contains two binding domains, one for the sites of
methylation themselves and the other for a flexible tether at the C
terminus of the receptor. We have explored the theoretical consequences
of this binding geometry for a CheR molecule associated with a cluster
of chemotactic receptors. Calculations show that the CheR molecule will
bind with high net affinity to the receptor lattice, having a high probability of being attached by one or both of its domains at any
instant of time. Because of the relatively low affinity of its
individual domains and the close proximity of neighboring receptors, it
is likely that when one domain unbinds it will reattach to the array
before the other domain unbinds. Stochastic simulations show that the
enzyme will move through the receptor cluster in a hand-over-hand
fashion, like a gibbon swinging through the branches of a tree. We
explore the possible consequences of this motion, which we term
"molecular brachiation", for chemotactic adaptation and suggest
that a similar mechanism may be operative in other large assemblies of
protein molecules.
Biophys J, April 2002, p. 1809-1817, Vol. 82, No. 4
© 2002 by the Biophysical Society 0006-3495/02/04/1809/09 $2.00
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