Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria
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Date
2022
Authors
Ahmed, Ishtiyaq
Hahn, Jeanette
Henrickson, Amy
Khaja, Faisal Tarique
Demeler, Borries
Dubnau, David
Neiditch, Matthew B.
Journal Title
Journal ISSN
Volume Title
Publisher
Springer Nature
Abstract
An essential step in bacterial transformation is the uptake of DNA into the periplasm, across the thick peptidoglycan cell wall of Gram-positive bacteria, or the outer membrane and thin peptidoglycan layer of Gram-negative bacteria. ComEA, a DNA-binding protein widely conserved in transformable bacteria, is required for this uptake step. Here we determine X-ray crystal structures of ComEA from two Gram-positive species, Bacillus subtilis and Geobacillus stearothermophilus, identifying a domain that is absent in Gram-negative bacteria. X-ray crystallographic, genetic, and analytical ultracentrifugation (AUC) analyses reveal that this domain drives ComEA oligomerization, which we show is required for transformation. We use multi-wavelength AUC (MW-AUC) to characterize the interaction between DNA and the ComEA DNA-binding domain. Finally, we present a model for the interaction of the ComEA DNA-binding domain with DNA, suggesting that ComEA oligomerization may provide a pulling force that drives DNA uptake across the thick cell walls of Gram-positive bacteria.
Description
Open access article. Creative Commons Attribution 4.0 Interntional license (CC BY 4.0) applies
Keywords
Bacterial genetics , Bacterial structural biology , ComEA , DNA-binding domain , Gram-positive , Gram-negative
Citation
Ahmed, I., Hahn, J., Henrickson, A., Khaja, F. T., Demeler, B., Dubnau, D., & Neiditch, M. B. (2022). Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria. Nature Communications, 13, Article 7724. https://doi.org/10.1038/s41467-022-35129-0