Isolation of human DNA sequences that bind to nuclear factor I, a host protein involved in adenovirus DNA replication.
- 1 July 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (13) , 4013-4017
- https://doi.org/10.1073/pnas.81.13.4013
Abstract
Nuclear factor I is a 47,000-dalton protein isolated from human cervical carcinoma HeLa cells that is required for the in vitro replication of adenovirus DNA. This protein was previously shown to bind specifically to nucleotides 17-48 of the left-hand terminus of cloned adenovirus serotype 5 DNA. An in vitro assay for DNA sequences that compete with adenovirus DNA for the binding of nuclear factor I was developed. With this assay, specific binding of human DNA sequences to nuclear factor I was shown. Using the DNA binding activity of nuclear factor I, segments of human DNA that bind tightly to this protein were isolated and cloned. One nuclear factor I binding site is present about every 100,000 base pairs in the HeLa cell genome. The binding of these DNA molecules to nuclear factor I resembles the binding of cloned adenovirus DNA to the protein and is resistant to high ionic strength. The isolation of DNA sequences from HeLa cells that bind specifically to nuclear factor I suggests that this protein interacts with host DNA in vivo.This publication has 34 references indexed in Scilit:
- A homogeneous type II DNA topoisomerase from HeLa cell nuclei.Journal of Biological Chemistry, 1981
- Eukaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei.Proceedings of the National Academy of Sciences, 1981
- Formation of a covalent complex between the 80,000-dalton adenovirus terminal protein and 5'-dCMP in vitro.Proceedings of the National Academy of Sciences, 1981
- Adenovirus DNA replication in vitro: characterization of a protein covalently linked to nascent DNA strands.Proceedings of the National Academy of Sciences, 1980
- Characterization of Drosophila DNA-binding protein DB-2: demonstration of its sequence-specific interaction with DNA.Proceedings of the National Academy of Sciences, 1980
- Transforming activity of DNA of chemically transformed and normal cellsNature, 1980
- Ubiquitous, interspersed repeated sequences in mammalian genomes.Proceedings of the National Academy of Sciences, 1980
- recA protein-catalyzed strand assimilation: stimulation by Escherichia coli single-stranded DNA-binding protein.Proceedings of the National Academy of Sciences, 1980
- Identification of a protein linked to the ends of adenovirus DNACell, 1977
- lac repressor-operator interaction: I. Equilibrium studiesJournal of Molecular Biology, 1970