Human mitochondrial DNA is packaged with TFAM
Top Cited Papers
- 15 March 2003
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 31 (6), 1640-1645
- https://doi.org/10.1093/nar/gkg251
Abstract
Mitochondrial transcription factor A (TFAM), a member of the high mobility group proteins, is essential for maintenance of mitochondrial DNA (mtDNA). Most TFAM and mtDNA (both of which are normally soluble) was recovered from the particulate fraction of human placental mitochondria when extracted with the non-ionic detergent Nonidet P-40. mtDNA and TFAM were co-immunoprecipitated by anti-TFAM antibodies. TFAM was released into the supernatant by DNase I digestion of mtDNA in the particulate fraction. Thus, TFAM and mtDNA are tightly associated with each other, and it is likely that few TFAM or mtDNA molecules exist in an unbound form in mitochondria. Based on the fact that TFAM is abundant enough to wrap mtDNA entirely, these results suggest that human mtDNA is packaged with TFAM.Keywords
This publication has 31 references indexed in Scilit:
- Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNANature Genetics, 2002
- Regulation of mitochondrial D‐loops by transcription factor A and single‐stranded DNA‐binding proteinEMBO Reports, 2002
- A Human Mitochondrial Transcription Factor Is Related to RNA Adenine Methyltransferases and Binds S-AdenosylmethionineMolecular and Cellular Biology, 2002
- Human mitochondrial DNA deletions associated with mutations in the gene encoding Twinkle, a phage T7 gene 4-like protein localized in mitochondriaNature Genetics, 2001
- Drosophila mitochondrial transcription factor A (d-TFAM) is dispensable for the transcription of mitochondrial DNA in Kc167 cellsBiochemical Journal, 2001
- In organello formaldehyde crosslinking of proteins to mtDNA: Identification of bifunctional proteinsProceedings of the National Academy of Sciences, 2000
- Binding of Human Mitochondrial Transcription Factor A, an HMG Box Protein, to a Four-Way DNA JunctionBiochemical and Biophysical Research Communications, 2000
- Architectural regulations and Hmg1Nature Genetics, 1999
- Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix proteinProceedings of the National Academy of Sciences, 1999
- Association of a protein structure of probable membrane derivation with HeLa cell mitochondrial DNA near its origin of replication.Proceedings of the National Academy of Sciences, 1977