Binding of human mitochondrial transcription factor A, an HMG box protein, to a four-way DNA junction

Tetsuji Ohno, Shuyo Umeda, Naotaka Hamasaki, Dongchon Kang

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Mitochondrial transcription factor A (mtTFA), the only known transcription factor in mitochondria, is also implicated in maintenance of mitochondrial genome although little is elucidated about its molecular basis. mtTFA is a member of HMG box proteins family. Some HMG proteins bind with high affinity to four-way DNA junctions that mimic a Holliday structure, a putative intermediate in DNA recombination. To explore possible involvement of a Holliday-like structure in the maintenance of mitochondrial genome, we examine the binding of recombinant human mtTFA to a synthetic four-way DNA junction. The human mtTFA binds to the four-way DNA junction with an approximately 10-fold higher affinity than to the corresponding linear duplex DNA and with essentially the same affinity as to a 40-mer DNA containing the human mitochondrial light strand promoter sequence. The mtTFA binds to the four-way as a monomer. Both of the two HMG box domains of human mtTFA are required for the high affinity binding to the four-way junction. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)492-498
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume271
Issue number2
DOIs
Publication statusPublished - May 10 2000

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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