Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria


  • The core challenge addressed is understanding how bacterial transformation works, particularly focusing on the process of DNA uptake into the periplasm of Gram-positive and Gram-negative bacteria. A central player in this process is ComEA, a DNA-binding protein essential for this uptake step. There are differences in the structures of ComEA in Gram-positive versus Gram-negative bacteria that are not yet understood, particularly a domain found in Gram-positive bacteria that drives ComEA oligomerization.


  • X-ray crystal structures of ComEA from two Gram-positive species, Bacillus subtilis and Geobacillus stearothermophilus, were determined. These structures revealed a domain absent in Gram-negative bacteria, which drives ComEA oligomerization.
  • Various analyses like X-ray crystallography, genetic, and analytical ultracentrifugation (AUC) were employed to investigate this domain's role.
  • Multi-wavelength AUC was used to study the interaction between DNA and the ComEA DNA-binding domain.
  • A model was proposed based on the collected data. The model suggests that the oligomerization of ComEA provides a pulling force, enabling DNA uptake across the thick cell walls of Gram-positive bacteria.


  • The research has revealed new structural and functional insights into ComEA, a protein central to bacterial transformation. The identified oligomerization domain in ComEA, specific to Gram-positive bacteria, is crucial for DNA uptake across their thick cell walls. This discovery advances our understanding of bacterial transformation and highlights the distinct molecular mechanisms employed by Gram-positive bacteria during this process.
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Comparability Studies
Material Science (metal nanoparticles, synthetic polymers, drug compounds)

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