Robustness in bacterial chemotaxis

Nature. 1999 Jan 14;397(6715):168-71. doi: 10.1038/16483.


Networks of interacting proteins orchestrate the responses of living cells to a variety of external stimuli, but how sensitive is the functioning of these protein networks to variations in their biochemical 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 robust; 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 systems. 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 architecture.

MeSH terms

  • Adaptation, Physiological
  • Bacterial Proteins / physiology
  • Chemotaxis / physiology*
  • Escherichia coli / physiology*
  • Methyltransferases / physiology


  • Bacterial Proteins
  • Methyltransferases
  • chemotaxis methyltransferase