The architects of bacterial DNA bridges: A structurally and functionally conserved family of proteins

L. Qin, A. M. Erkelens, F. Ben Bdira, R. T. Dame*

*Corresponding author for this work

Research output: Contribution to JournalReview articleAcademicpeer-review


Every organism across the tree of life compacts and organizes its genome with architectural chromatin proteins. While eukaryotes and archaea express histone proteins, the organization of bacterial chromosomes is dependent on nucleoid-associated proteins. In Escherichia coli and other proteobacteria, the histone-like nucleoid structuring protein (H-NS) acts as a global genome organizer and gene regulator. Functional analogues of H-NS have been found in other bacterial species: MvaT in Pseudomonas species, Lsr2 in actinomycetes and Rok in Bacillus species. These proteins complement hns phenotypes and have similar DNA-binding properties, despite their lack of sequence homology. In this review, we focus on the structural and functional characteristics of these four architectural proteins. They are able to bridge DNA duplexes, which is key to genome compaction, gene regulation and their response to changing conditions in the environment. Structurally the domain organization and charge distribution of these proteins are conserved, which we suggest is at the basis of their conserved environment responsive behaviour. These observations could be used to find and validate new members of this protein family and to predict their response to environmental changes.

Original languageEnglish
Article number190223
JournalOpen Biology
Issue number12
Publication statusPublished - 1 Dec 2019
Externally publishedYes


  • Bacterial chromatin
  • Environmental sensing
  • Horizontal gene transfer
  • Nucleoid


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