ArticleBiophysical journal2004
Mechanism of DNA compaction by yeast mitochondrial protein Abf2p.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 63 citations in OpenAlex.
- Sequence-specific dynamic DNA bending explains mitochondrial TFAM's dual role in DNA packaging and transcription initiation.Nature communications · 2024Article
- Two mitochondrial HMG-box proteins, Cim1 and Abf2, antagonistically regulate mtDNA copy number in Saccharomyces cerevisiae.Nucleic acids research · 2023Article
- Structural analysis of the Candida albicans mitochondrial DNA maintenance factor Gcf1p reveals a dynamic DNA-bridging mechanism.Nucleic acids research · 2023Article
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases.Biomolecules · 2020Review
- Organization of DNA in Mammalian Mitochondria.International journal of molecular sciences · 2019Review
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
- Accurate nanoscale flexibility measurement of DNA and DNA-protein complexes by atomic force microscopy in liquid.Nanoscale · 2017Article
- Single-molecule studies of high-mobility group B architectural DNA bending proteins.Biophysical reviews · 2017Review
- DNA structure directs positioning of the mitochondrial genome packaging protein Abf2p.Nucleic acids research · 2017Article
- Organization and dynamics of yeast mitochondrial nucleoids.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of mitochondrial nucleoids.Bioscience reports · 2015Article
- Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The strictly aerobic yeast Yarrowia lipolytica tolerates loss of a mitochondrial DNA-packaging protein.Eukaryotic cell · 2014Article
- DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin.Nucleic acids research · 2014Article
- TbKAP6, a mitochondrial HMG box-containing protein in Trypanosoma brucei, is the first trypanosomatid kinetoplast-associated protein essential for kinetoplast DNA replication and maintenance.Eukaryotic cell · 2014Article
- Mechanism of homologous recombination and implications for aging-related deletions in mitochondrial DNA.Microbiology and molecular biology reviews : MMBR · 2013Review
- Attractive hydration forces in DNA-dendrimer interactions on the nanometer scale.The journal of physical chemistry. B · 2013Article
- Protein sliding and DNA denaturation are essential for DNA organization by human mitochondrial transcription factor A.Nature communications · 2012Article
- Superresolution fluorescence imaging of mitochondrial nucleoids reveals their spatial range, limits, and membrane interaction.Molecular and cellular biology · 2011Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We used high-resolution atomic force microscopy to image the compaction of linear and circular DNA by the yeast mitochondrial protein Abf2p, which plays a major role in packaging mitochondrial DNA. Atomic force microscopy images show that protein binding induces drastic bends in the DNA backbone for both linear and circular DNA. At a high concentration of Abf2p DNA collapses into a tight nucleoprotein complex. We quantified the compaction of linear DNA by measuring the end-to-end distance of the DNA molecule at increasing concentrations of Abf2p. We also derived a polymer statistical mechanics model that provides a quantitative description of compaction observed in our experiments. This model shows that sharp bends in the DNA backbone are often sufficient to cause DNA compaction. Comparison of our model with the experimental data showed excellent quantitative correlation and allowed us to determine binding characteristics for Abf2p. These studies indicate that Abf2p compacts DNA through a simple mechanism that involves bending of the DNA backbone. We discuss the implications of such a mechanism for mitochondrial DNA maintenance and organization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.