Spatial Restrictions in Chemotaxis Signaling Arrays: A Role for Chemoreceptor Flexible Hinges across Bacterial Diversity

Int J Mol Sci. 2019 Jun 19;20(12):2989. doi: 10.3390/ijms20122989.

Abstract

The chemotactic sensory system enables motile bacteria to move toward favorable environments. Throughout bacterial diversity, the chemoreceptors that mediate chemotaxis are clustered into densely packed arrays of signaling complexes. In these arrays, rod-shaped receptors are in close proximity, resulting in limited options for orientations. A recent geometric analysis of these limitations in Escherichia coli, using published dimensions and angles, revealed that in this species, straight chemoreceptors would not fit into the available space, but receptors bent at one or both of the recently-documented flexible hinges would fit, albeit over a narrow window of shallow bend angles. We have now expanded our geometric analysis to consider variations in receptor length, orientation and placement, and thus to species in which those parameters are known to be, or might be, different, as well as to the possibility of dynamic variation in those parameters. The results identified significant limitations on the allowed combinations of chemoreceptor dimensions, orientations and placement. For most combinations, these limitations excluded straight chemoreceptors, but allowed receptors bent at a flexible hinge. Thus, our analysis identifies across bacterial diversity a crucial role for chemoreceptor flexible hinges, in accommodating the limitations of molecular crowding in chemotaxis core signaling complexes and their arrays.

Keywords: Bacterial chemotaxis; helical bends; molecular crowding; transmembrane receptors.

MeSH terms

  • Bacterial Physiological Phenomena*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Chemotaxis*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Protein Binding
  • Protein Multimerization
  • Signal Transduction*
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • Membrane Proteins