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Nucleic Acids Research, 2003, Vol. 31, No. 6 1640-1645
© 2003 Oxford University Press

Human mitochondrial DNA is packaged with TFAM

Tanfis Istiaq Alam, Tomotake Kanki, Tsuyoshi Muta, Koutarou Ukaji, Yoshito Abe, Hiroshi Nakayama1, Koji Takio1, Naotaka Hamasaki and Dongchon Kang

Department of Clinical Chemistry and Laboratory Medicine, Kyushu University Graduate School of Medical Sciences, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan and 1 Biomolecular Characterization Division, RIKEN (The Institute for Physical and Chemical Research), Wako 351-0198, Japan

*To whom correspondence should be addressed. Tel: +81 92 642 5749; Fax: +81 92 642 5772; Email: kang{at}mailserver.med.kyushu-u.ac.jp

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.


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