Related Experiment Video
Updated: Aug 19, 2026

Two- and Three-Dimensional Live Cell Imaging of DNA Damage Response Proteins
Published on: September 28, 2012
P53 physically interacts with mitochondrial transcription factor A and differentially regulates binding to damaged
Yoichiro Yoshida1, Hiroto Izumi, Takayuki Torigoe
1Department of Molecular Biology, University of Occupational and Environmental Health, School of Medicine, Kitakyushu Fukuoka 807-8555, Japan.
Abstract:
Mitochondrial transcription factor A (mtTFA; also designated Tfam) is necessary for both transcription and maintenance of mitochondrial DNA. mtTFA preferentially recognizes cisplatin-damaged DNA, as well as oxidized DNA. Increased apoptosis has been observed in mtTFA knockout animals, suggesting that mtTFA is involved in apoptosis. A fraction of p53 protein localizes to mitochondria at the onset of p53-dependent apoptosis, but not during p53-independent apoptosis. Using immunochemical coprecipitation, we observed binding of mtTFA and p53. Interaction between mtTFA and p53 required the high mobility group-box1 or high mobility group-box2 of mtTFA and amino acids 363-376 of p53. Binding of mtTFA to cisplatin-modified DNA was significantly enhanced by p53, whereas binding to oxidized DNA was inhibited. Our findings suggest that the interaction of p53 with mtTFA may play an important role in apoptosis.
Related Concept Videos
Negative Regulator Molecules
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
DNA Damage can Stall the Cell Cycle
Abnormal Proliferation
Interactions Between Signaling Pathways
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
DNA Damage Can Stall the Cell Cycle

