ArticleNucleic acids research2014
DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 62 citations in OpenAlex.
- Measuring bridging forces in protein-DNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Protamine-Mediated Tangles Produce Extreme Deoxyribonucleic Acid Compaction.Journal of the American Chemical Society · 2024Article
- Complexes of HMO1 with DNA: Structure and Affinity.Biomolecules · 2024Article
- Hmo1: A versatile member of the high mobility group box family of chromosomal architecture proteins.World journal of biological chemistry · 2024Review
- Atomic Force Microscopy Characterization of Reconstituted Protein-DNA Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Quantitative Determination of DNA Bridging Efficiency of Chromatin Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Multiple modes of DNA compaction by protamine.bioRxiv : the preprint server for biology · 2023Article
- Single-molecule study reveals Hmo1, not Hho1, promotes chromatin assembly in budding yeast.mBio · 2023Article
- HmbC, a Protein of the HMG Family, Participates in the Regulation of Carotenoid Biosynthesis inGenes · 2023Article
- Targeting of Hmo1 to subcompartments of the budding yeast nucleolus.Molecular biology of the cell · 2023Article
- Human FACT subunits coordinate to catalyze both disassembly and reassembly of nucleosomes.Cell reports · 2022Article
- Article
- Establishment and Maintenance of Open Ribosomal RNA Gene Chromatin States in Eukaryotes.Methods in molecular biology (Clifton, N.J.) · 2022Review
- The rDNA is biomolecular condensate formed by polymer-polymer phase separation and is sequestered in the nucleolus by transcription and R-loops.Nucleic acids research · 2021Article
- Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiae.PLoS genetics · 2020Article
- Bending and looping of long DNA by Polycomb repressive complex 2 revealed by AFM imaging in liquid.Nucleic acids research · 2020Article
- Promotion of Hyperthermic-Induced rDNA Hypercondensation inGenetics · 2020Article
- Article
- DP-BINDER: machine learning model for prediction of DNA-binding proteins by fusing evolutionary and physicochemical information.Journal of computer-aided molecular design · 2019Article
- Evidence for a bind-then-bend mechanism for architectural DNA binding protein yNhp6A.Nucleic acids research · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The regulation of chromatin structure in eukaryotic cells involves abundant architectural factors such as high mobility group B (HMGB) proteins. It is not understood how these factors control the interplay between genome accessibility and compaction. In vivo, HMO1 binds the promoter and coding regions of most ribosomal RNA genes, facilitating transcription and possibly stabilizing chromatin in the absence of histones. To understand how HMO1 performs these functions, we combine single molecule stretching and atomic force microscopy (AFM). By stretching HMO1-bound DNA, we demonstrate a hierarchical organization of interactions, in which HMO1 initially compacts DNA on a timescale of seconds, followed by bridge formation and stabilization of DNA loops on a timescale of minutes. AFM experiments demonstrate DNA bridging between strands as well as looping by HMO1. Our results support a model in which HMO1 maintains the stability of nucleosome-free chromatin regions by forming complex and dynamic DNA structures mediated by protein-protein interactions.
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