ArticleNucleic acids research2017
DNA structure directs positioning of the mitochondrial genome packaging protein Abf2p.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- The ISW1 and CHD1 chromatin remodelers suppress global nucleosome dynamics in living yeast cells.Science advances · 2025Article
- Phase separation in mitochondrial fate and mitochondrial diseases.Proceedings of the National Academy of Sciences of the United States of America · 2025Review
- Epigenetic Threads of Neurodegeneration: TFAM's Intricate Role in Mitochondrial Transcription.CNS & neurological disorders drug targets · 2025Review
- Probing mechanical selection in diverse eukaryotic genomes through accurate prediction of 3D DNA mechanics.bioRxiv : the preprint server for biology · 2024Article
- Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024Review
- 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
- A minimal motif for sequence recognition by mitochondrial transcription factor A (TFAM).Nucleic acids research · 2022Article
- Insight into the sequence-specific elements leading to increased DNA bending and ligase-mediated circularization propensity by antitumor trabectedin.Journal of computer-aided molecular design · 2021Article
- HBD1 protein with a tandem repeat of two HMG-box domains is a DNA clip to organize chloroplast nucleoids inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure, mechanism, and regulation of mitochondrial DNA transcription initiation.The Journal of biological chemistry · 2020Review
- Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases.Biomolecules · 2020Review
- Diversity and Postzygotic Evolution of the Mitochondrial Genome in Hybrids ofFrontiers in microbiology · 2020Article
- New protein-DNA complexes in archaea: a small monomeric protein induces a sharp V-turn DNA structure.Scientific reports · 2019Article
- DNA specificities modulate the binding of human transcription factor A to mitochondrial DNA control region.Nucleic acids research · 2019Article
- 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
- Organization and dynamics of yeast mitochondrial nucleoids.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
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Authors and funding
9 authors at 3 institutions in 1 country.
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Abstract
The mitochondrial genome (mtDNA) is assembled into nucleo-protein structures termed nucleoids and maintained differently compared to nuclear DNA, the involved molecular basis remaining poorly understood. In yeast (Saccharomyces cerevisiae), mtDNA is a ∼80 kbp linear molecule and Abf2p, a double HMG-box protein, packages and maintains it. The protein binds DNA in a non-sequence-specific manner, but displays a distinct 'phased-binding' at specific DNA sequences containing poly-adenine tracts (A-tracts). We present here two crystal structures of Abf2p in complex with mtDNA-derived fragments bearing A-tracts. Each HMG-box of Abf2p induces a 90° bend in the contacted DNA, causing an overall U-turn. Together with previous data, this suggests that U-turn formation is the universal mechanism underlying mtDNA compaction induced by HMG-box proteins. Combining this structural information with mutational, biophysical and computational analyses, we reveal a unique DNA binding mechanism for Abf2p where a characteristic N-terminal flag and helix are crucial for mtDNA maintenance. Additionally, we provide the molecular basis for A-tract mediated exclusion of Abf2p binding. Due to high prevalence of A-tracts in yeast mtDNA, this has critical relevance for nucleoid architecture. Therefore, an unprecedented A-tract mediated protein positioning mechanism regulates DNA packaging proteins in the mitochondria, and in combination with DNA-bending and U-turn formation, governs mtDNA compaction.
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