Bacterial protein HU dictates the morphology of DNA condensates produced by crowding agents and polyamines.

TitleBacterial protein HU dictates the morphology of DNA condensates produced by crowding agents and polyamines.
Publication TypeJournal Article
Year of Publication2007
AuthorsSarkar, T, Vitoc, I, Mukerji, I, Hud, NV
JournalNucleic Acids Res
Date Published2007
KeywordsDNA, DNA, Superhelical, DNA-Binding Proteins, Escherichia coli Proteins, Models, Biological, Polyethylene Glycols, Spermidine, Surface-Active Agents

Controlling the size and shape of DNA condensates is important in vivo and for the improvement of nonviral gene delivery. Here, we demonstrate that the morphology of DNA condensates, formed under a variety of conditions, is shifted completely from toroids to rods if the bacterial protein HU is present during condensation. HU is a non-sequence-specific DNA binding protein that sharply bends DNA, but alone does not condense DNA into densely packed particles. Less than one HU dimer per 225 bp of DNA is sufficient to completely control condensate morphology when DNA is condensed by spermidine. We propose that rods are favored in the presence of HU because rods contain sharply bent DNA, whereas toroids contain only smoothly bent DNA. The results presented illustrate the utility of naturally derived proteins for controlling the shape of DNA condensates formed in vitro. HU is a highly conserved protein in bacteria that is implicated in the compaction and shaping of nucleoid structure. However, the exact role of HU in chromosome compaction is not well understood. Our demonstration that HU governs DNA condensation in vitro also suggests a mechanism by which HU could act as an architectural protein for bacterial chromosome compaction and organization in vivo.

Alternate JournalNucleic Acids Res.
PubMed ID17259223
PubMed Central IDPMC1807954
Grant ListGM62873 / GM / NIGMS NIH HHS / United States