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X-ray crystal structure of Bacillus subtilis ComEA
Structural highlights
FunctionCOMEA_BACSU Needed for both DNA binding and transport. It is absolutely required for the uptake of transforming DNA but not for binding. Its role in binding may be indirect.[1] Publication Abstract from PubMedAn 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. Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria.,Ahmed I, Hahn J, Henrickson A, Khaja FT, Demeler B, Dubnau D, Neiditch MB Nat Commun. 2022 Dec 13;13(1):7724. doi: 10.1038/s41467-022-35129-0. PMID:36513643[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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