Letters to Nature

Nature 397, 168-171 (14 January 1999) | doi:10.1038/16483; Received 13 October 1998; Accepted 27 November 1998

Robustness in bacterial chemotaxis

U. Alon1,2, M. G. Surette3, N. Barkai2 & S. Leibler1,2

  1. Departments of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA
  2. Departments of Physics, Princeton University, Princeton, New Jersey 08544, USA
  3. Department of Microbiology and Infectious Diseases, Calgary, Alberta, Canada T2N 4N1

Correspondence to: S. Leibler1,2 Correspondence and requests for materials should be addressed to S.L. (e-mail: Email: leibler@princeton.edu).

Networks of interacting proteins orchestrate the responses of living cells to a variety of external stimuli1, but how sensitive is the functioning of these protein networks to variations in theirbiochemical parameters? One possibility is that to achieve appropriate function, the reaction rate constants and enzyme concentrations need to be adjusted in a precise manner, and any deviation from these 'fine-tuned' values ruins the network's performance. An alternative possibility is that key properties of biochemical networks are robust2; that is, they are insensitive to the precise values of the biochemical parameters. Here we address this issue in experiments using chemotaxis of Escherichia coli, one of the best-characterized sensory systems3,4. We focus on how response and adaptation to attractant signals vary with systematic changes in the intracellular concentration of the components of the chemotaxis network. We find that some properties, such as steady-state behaviour and adaptation time, show strong variations in response to varying protein concentrations. In contrast, the precision of adaptation is robust and does not vary with the protein concentrations. This is consistent with a recently proposed molecular mechanism for exact adaptation, where robustness is a direct consequence of the network's architecture2.