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Inch by inch, row by row

Nature Structural & Molecular Biology volume 13, pages 382–384 (2006)Cite this article

Bacterial chemotaxis systems have cooperatively interacting clusters of transmembrane receptors and signaling proteins to detect, amplify, integrate and adapt to environmental signals. A recent study provides experimental data to construct a new model of the signaling complex.

In recent years, it has become clear that the transmembrane receptor proteins in bacterial chemotaxis signaling systems have the properties of a two-dimensional interactive array, where the receptors and the intracellular signaling proteins often localize in clusters at the cell poles1. The organization of the array and the way it adapts to variations in the environmental conditions is an intriguing and significant puzzle, as these features lie at the heart of the pathway's remarkable properties of signal integration and high sensitivity over a broad range of chemoeffector concentrations2,3. So, the solution to the puzzle has become a question of determining how, angstrom by angstrom, the receptor array assembles and behaves. On page 400 of this issue, Park et al.4 have not only added to the bounty of protein structures but also generated a new model for the receptor–kinase signaling complex, using an approach that is based on the measurement of interdomain distances by pulsed EPR. The new model is testable and will drive the design of new studies.

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Figure 1: Two models for two-dimensional chemotaxis receptor arrays, viewed from a perspective looking down from the membrane into the cytoplasm.

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  1. the Department of Chemistry, The University of Massachusetts Amherst, 710 North Pleasant St, Amherst, 01003-9336, Massachusetts, USA

    Robert M Weis

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Weis, R. Inch by inch, row by row. Nat Struct Mol Biol 13, 382–384 (2006). https://doi.org/10.1038/nsmb0506-382

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