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

Ishtiyaq Ahmed, Jeanette Hahn, Amy Henrickson, Faisal Tarique Khaja, Borries Demeler, David Dubnau, Matthew B. Neiditch

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article number7724
JournalNature Communications
Volume13
Issue number1
DOIs
StatePublished - Dec 2022

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