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

Simple item page
dc.contributor.authorAhmed, Ishtiyaq
dc.contributor.authorHahn, Jeanette
dc.contributor.authorHenrickson, Amy
dc.contributor.authorKhaja, Faisal Tarique
dc.contributor.authorDemeler, Borries
dc.contributor.authorDubnau, David
dc.contributor.authorNeiditch, Matthew B.
dc.date.accessioned2024-08-20T19:56:30Z
dc.date.available2024-08-20T19:56:30Z
dc.date.issued2022
dc.descriptionOpen access article. Creative Commons Attribution 4.0 Interntional license (CC BY 4.0) applies
dc.description.abstractAn 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.
dc.description.peer-reviewYes
dc.identifier.citationAhmed, 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
dc.identifier.urihttps://hdl.handle.net/10133/6872
dc.language.isoen
dc.publisherSpringer Nature
dc.publisher.departmentDepartment of Chemistry and Biochemistry
dc.publisher.facultyArts and Science
dc.publisher.institutionRutgers Biomedical Health Sciences
dc.publisher.institutionUniversity of Lethbridge
dc.publisher.institutionUniversity of Texas Health at San Antonio
dc.publisher.institutionUniversity of Montana
dc.publisher.urlhttps://doi.org/10.1038/s41467-022-35129-0
dc.subjectBacterial genetics
dc.subjectBacterial structural biology
dc.subjectComEA
dc.subjectDNA-binding domain
dc.subjectGram-positive
dc.subjectGram-negative
dc.subject.lcshBacterial transformation
dc.subject.lcshDNA-binding proteins
dc.subject.lcshOligomerization
dc.subject.lcshGram-positive bacteria
dc.subject.lcshGram-negative bacteria
dc.titleStructure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria
dc.typeArticle
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Demeler-structure-function.pdf
Size:
5.22 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.75 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Demeler, Borries