ArticleNucleic acids research2007
Bacterial protein HU dictates the morphology of DNA condensates produced by crowding agents and polyamines.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Polyphosphate: The "Dark Matter" of Bacterial Chromatin Structure.Molecular microbiology · 2025Review
- Extracellular DNA-protein interactions.Current opinion in structural biology · 2024Review
- An evolutionarily conserved metabolite inhibits biofilm formation in Escherichia coli K-12.Nature communications · 2024Article
- Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom.Transcription · 2021Review
- Single-molecule tracking reveals that the nucleoid-associated protein HU plays a dual role in maintaining proper nucleoid volume through differential interactions with chromosomal DNA.Molecular microbiology · 2021Article
- Protamine loops DNA in multiple steps.Nucleic acids research · 2020Article
- Single-molecule visualization of the effects of ionic strength and crowding on structure-mediated interactions in supercoiled DNA molecules.Nucleic acids research · 2019Article
- Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging.Nature reviews. Microbiology · 2014Review
- A histone-like protein induces plasmid DNA to form liquid crystals in vitro and gene compaction in vivo.International journal of molecular sciences · 2013Article
- Double-Strand Break Repair and Holliday Junction Processing Are Required for Chromosome Processing in Stationary-Phase Escherichia coli Cells.G3 (Bethesda, Md.) · 2011Article
- Understanding apparent DNA flexibility enhancement by HU and HMGB architectural proteins.Journal of molecular biology · 2011Article
- Super-resolution imaging of the nucleoid-associated protein HU in Caulobacter crescentus.Biophysical journal · 2011Article
- Effects of the nucleoid protein HU on the structure, flexibility, and ring-closure properties of DNA deduced from Monte Carlo simulations.Journal of molecular biology · 2008Article
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4 authors.
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Abstract
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.
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