TY - JOUR
T1 - Binding of the universal minicircle sequence binding protein at the kinetoplast DNA replication origin
AU - Onn, Itay
AU - Kapeller, Irit
AU - Abu-Elneel, Kawther
AU - Shlomai, Joseph
PY - 2006/12/8
Y1 - 2006/12/8
N2 - Kinetoplast DNA, the mitochondrial DNA of trypanosomatids, is a remarkable DNA structure that contains, in the species Crithidia fasciculata, 5000 topologically linked duplex DNA minicircles. Their replication initiates at two conserved sequences, a dodecamer, known as the universal minicircle sequence (UMS), and a hexamer, which are located at the replication origins of the minicircle L and H strands, respectively. A UMS-binding protein (UMSBP) binds specifically the 12-mer UMS sequence and a 14-mer sequence that contains the conserved hexamer in their single-stranded DNA conformation. In vivo cross-linking analyses reveal the binding of UMSBP to kinetoplast DNA networks in the cell. Furthermore, UMSBP binds in vitro to native minicircle origin fragments, carrying the UMSBP recognition sequences. UMSBP binding at the replication origin induces conformational changes in the bound DNA through its folding, aggregation and condensation.
AB - Kinetoplast DNA, the mitochondrial DNA of trypanosomatids, is a remarkable DNA structure that contains, in the species Crithidia fasciculata, 5000 topologically linked duplex DNA minicircles. Their replication initiates at two conserved sequences, a dodecamer, known as the universal minicircle sequence (UMS), and a hexamer, which are located at the replication origins of the minicircle L and H strands, respectively. A UMS-binding protein (UMSBP) binds specifically the 12-mer UMS sequence and a 14-mer sequence that contains the conserved hexamer in their single-stranded DNA conformation. In vivo cross-linking analyses reveal the binding of UMSBP to kinetoplast DNA networks in the cell. Furthermore, UMSBP binds in vitro to native minicircle origin fragments, carrying the UMSBP recognition sequences. UMSBP binding at the replication origin induces conformational changes in the bound DNA through its folding, aggregation and condensation.
UR - http://www.scopus.com/inward/record.url?scp=33846025784&partnerID=8YFLogxK
U2 - 10.1074/jbc.M606374200
DO - 10.1074/jbc.M606374200
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C2 - 17046830
AN - SCOPUS:33846025784
SN - 0021-9258
VL - 281
SP - 37468
EP - 37476
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 49
ER -