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 language | English |
|---|---|
| Pages (from-to) | 492-498 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 271 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - May 10 2000 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Binding of human mitochondrial transcription factor A, an HMG box protein, to a four-way DNA junction. / Ohno, Tetsuji; Umeda, Shuyo; Hamasaki, Naotaka; Kang, Dongchon.
In: Biochemical and Biophysical Research Communications, Vol. 271, No. 2, 10.05.2000, p. 492-498.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding of human mitochondrial transcription factor A, an HMG box protein, to a four-way DNA junction
AU - Ohno, Tetsuji
AU - Umeda, Shuyo
AU - Hamasaki, Naotaka
AU - Kang, Dongchon
PY - 2000/5/10
Y1 - 2000/5/10
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0034630725&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2000.2656
DO - 10.1006/bbrc.2000.2656
M3 - Article
C2 - 10799324
AN - SCOPUS:0034630725
VL - 271
SP - 492
EP - 498
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -