Journal
GENES TO CELLS
Volume 20, Issue 12, Pages 1017-1027Publisher
WILEY-BLACKWELL
DOI: 10.1111/gtc.12306
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan (JSPS KAKENHI) [24790324, 15K19029]
- Program for the Strategic Research Foundation at Private Universities from the Ministry of Education, Culture, Sports, Science and Technology of Japan
- JKA through KEIRIN RACE
- Grants-in-Aid for Scientific Research [24790324, 15K19029] Funding Source: KAKEN
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Mitochondrial transcription factor A (TFAM) is a key regulator of mitochondrial DNA (mtDNA). TFAM interacts with itself and forms dimers; however, the precise interaction domain in vivo has not yet been determined. We herein showed that human TFAM formed oligomers in mitochondria by in situ chemical cross-linking. We used the separated fluorescent protein, monomeric Kusabira-Green, as a reporter to monitor their self-association in mitochondria. This reporter successfully detected the TFAM-TFAM interaction in cells as fluorescent signals on mitochondria. We also found that the N-terminal high-mobility group box domain was sufficient for this interaction. The expression of the dimer-defective mutant induced enlarged mtDNA nucleoids, suggesting the importance of dimerization in the distribution of mtDNA. The reporter system also supported the association and mixture between independent nucleoids through TFAM by a cell fusion assay using hemagglutinating virus of Japan. We here, for the first time, visualized the interaction of TFAM molecules in mitochondria and proposed its implications for the dynamics of mtDNA nucleoids.
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