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Nucleic Acids Res
1993 Feb 25;214:811-6. doi: 10.1093/nar/21.4.811.
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Characterization of a high-affinity binding site for a DNA-binding protein from sea urchin embryo mitochondria.
Qureshi SA
,
Jacobs HT
.
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Based on electrophoretic mobility shift assays, DNase I footprinting and modification interference analyses we have identified a sequence-specific DNA-binding protein in blastula stage mitochondria of the sea urchin Strongylocentrotus purpuratus, which interacts with a binding site around the major pause site for DNA replication. This region straddles the boundary of the genes for ATP synthase subunit 6 and cytochrome c oxidase subunit III, and contains also a prominent origin of lagging-strand synthesis. The protein is thermostable, and its natural high-affinity binding site comprises the sequence 5''-AGCCT(N7)AGCAT-3''. Binding studies have demonstrated that two copies of the imperfect repeat, as well as the 7 bp spacing between them, are essential for tight binding. Based on the location of its binding site, we tentatively designate the protein mitochondrial pause-region binding protein (mtPBP) 1.
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