ArticleNucleic acids research2009
Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
52 citing papers in PubMed, 94 citations in OpenAlex.
- TFAM organizes DNA into compact higher order structures.bioRxiv : the preprint server for biology · 2026Article
- Mitochondrial transcription factor A: linking mtDNA maintenance, mitochondrial stress responses, and inflammaging.Frontiers in aging · 2026Review
- DNA sequence and lesion-dependent mitochondrial transcription factor A (TFAM)-DNA-binding modulates DNA repair activities and products.Nucleic acids research · 2024Article
- BiallelicHeliyon · 2024Article
- Mechanisms and regulation of human mitochondrial transcription.Nature reviews. Molecular cell biology · 2024Review
- Adenovirus protein VII binds the A-box of HMGB1 to repress interferon responses.PLoS pathogens · 2023Article
- Article
- Structural analysis of the Candida albicans mitochondrial DNA maintenance factor Gcf1p reveals a dynamic DNA-bridging mechanism.Nucleic acids research · 2023Article
- 35 Years of TFAM Research: Old Protein, New Puzzles.Biology · 2023Review
- The C-Terminal Tail of Mitochondrial Transcription Factor A Is Dispensable for Mitochondrial DNA Replication and Transcription In Situ.International journal of molecular sciences · 2023Article
- A minimal motif for sequence recognition by mitochondrial transcription factor A (TFAM).Nucleic acids research · 2022Article
- Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A.Frontiers in cell and developmental biology · 2022Article
- Mitochondrial Transcription Factor A Binds to and Promotes Mutagenic Transcriptional Bypass ofAnalytical chemistry · 2021Article
- Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases.Biomolecules · 2020Review
- 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
- Cytosine methylation of mitochondrial DNA at CpG sequences impacts transcription factor A DNA binding and transcription.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019Article
- Structural basis of mitochondrial transcription.Nature structural & molecular biology · 2018Review
- Protein Flexibility and Synergy of HMG Domains Underlie U-Turn Bending of DNA by TFAM in Solution.Biophysical journal · 2018Article
- Acetylation and phosphorylation of human TFAM regulate TFAM-DNA interactions via contrasting mechanisms.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The mitochondrial transcription factor A (mtTFA) is central to assembly and initiation of the mitochondrial transcription complex. Human mtTFA (h-mtTFA) is a dual high mobility group box (HMGB) protein that binds site-specifically to the mitochondrial genome and demarcates the promoters for recruitment of h-mtTFB1, h-mtTFB2 and the mitochondrial RNA polymerase. The stoichiometry of h-mtTFA was found to be a monomer in the absence of DNA, whereas it formed a dimer in the complex with the light strand promoter (LSP) DNA. Each of the HMG boxes and the C-terminal tail were evaluated for their ability to bind to the LSP DNA. Removal of the C-terminal tail only slightly decreased nonsequence specific DNA binding, and box A, but not box B, was capable of binding to the LSP DNA. The X-ray crystal structure of h-mtTFA box B, at 1.35 A resolution, revealed the features of a noncanonical HMG box. Interactions of box B with other regions of h-mtTFA were observed. Together, these results provide an explanation for the unusual DNA-binding properties of box B and suggest possible roles for this domain in transcription complex assembly.
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Registered trials
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.