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

doi:10.1038/s41467-022-35129-0

Nature Communications (Dec 2022)

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

Affiliations

Ishtiyaq Ahmed: Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers Biomedical Health Sciences
Jeanette Hahn: Public Health Research Institute, Rutgers Biomedical Health Sciences
Amy Henrickson: Department of Chemistry and Biochemistry, University of Lethbridge
Faisal Tarique Khaja: Greehey Children’s Cancer Research Institute, University of Texas Health at San Antonio
Borries Demeler: Department of Chemistry and Biochemistry, University of Lethbridge
David Dubnau: Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers Biomedical Health Sciences
Matthew B. Neiditch: Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers Biomedical Health Sciences

DOI: https://doi.org/10.1038/s41467-022-35129-0
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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ComEA is a DNA-binding protein required for DNA uptake during bacterial transformation. Here, Ahmed et al. determine X-ray crystal structures of ComEA from Gram-positive bacteria, identifying a domain that is absent in Gram-negative bacteria and drives ComEA oligomerization, which is required for transformation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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