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Results for “DNA replication origin”

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At least 433 records · Page 24Linked to original sources
PubMed1998

DNA loop anchorage region colocalizes with the replication origin located downstream to the human gene encoding lamin B2.

The recently developed procedure of topoisomerase II-mediated DNA loop excision has been used to analyze the topological organization of a human genome fragment containing the gene encoding lamin B2 and the ppv1 gene. A 3.5 kb long DNA loop anchorage/topoisomerase II cleavage region was found within the area under study. This region includes the end of the lamin B2 coding unit and an intergenic region where an origin of DNA replication was previously found. These observations further corroborate the hypothesis that DNA replication origins are located at or close to DNA loop anchorage regions.

Binding Sites↗
PubMed1984

Nucleotide sequence of the Galleria mellonella nuclear polyhedrosis virus origin of DNA replication.

The initiation sites of the Galleria mellonella L. nuclear polyhedrosis virus (G.m. NPV) DNA replication were revealed. For this purpose SCLd 135 cells permitting the G.m. NPV productive reproduction were transformed by the recombinant plasmids containing the viral genome individual fragments in pRSF 2124 and pBR 322 vectors. It was revealed that 2 of the 32 recombinant plasmids can autonomously replicate in the eucaryotic cells. According to the Maxam-Gilbert method the DNA G.m. NPV fragment (1300 bp) primary structure of pHBR plasmid was determined. The structure analysis revealed the typical regulator signals as in the replicons. The possible regulation mechanism of the DNA G.m. NPV synthesis initiation was supposed.

Base Sequence↗
PubMed1979

Structure of the 3' hairpin termini of four rodent parvovirus genomes: nucleotide sequence homology at origins of DNA replication.

The nucleotide sequences of the 3' termini of the DNA from four autonomous rodent parvoviruses have been determined. The terminus of each genome exists as a Y-shaped hairpin structure involving 115 or 116 nucleotides. The sequence of this region of DNA is highly conserved and shows no evidence of internal sequence heterogeneity, a characteristic which is observed in the terminal nucleotide sequence of the helper-dependent, adeno-associated viruses (Berns et al., 1978a). The implications of these results with respect to the models of parvovirus DNA replication are discussed.

Base Sequence↗
PubMed1983

Specific binding of a cellular DNA replication protein to the origin of replication of adenovirus DNA.

Nuclear factor I, a 47-kilodalton protein, purified from nuclear extracts of uninfected HeLa cells, is involved in the initiation and possibly the elongation of replicating adenovirus (Ad) DNA in vitro. The binding of nuclear factor I to DNA has been monitored by a filter binding assay of nuclear factor I to DNA has been monitored by a filter binding assay using plasmid pLA1 DNA, which contains a 3,290 base-pair fragment derived from the left-hand terminus (coordinates, 0-9.4 map units) of Ad serotype 5 DNA. Nuclear factor I binds selectively to a double-stranded fragment spanning nucleotides 0-451 to the Ad genome. The retention of the 451-base-pair DNA fragment-nuclear factor I complex on nitrocellulose filters does not require Mg2+ or ATP and is resistant to high ionic strength. DNase I protection experiments revealed that nuclear factor I binds to a nucleotide sequence located at position 17-48, close to the terminus of Ad DNA. This 32-nucleotide sequence contains four "consensus" sequences present in various serotypes of Ad DNA and is capable of forming higher ordered structures. The role of nuclear factor I and this DNA sequence in the generation of Ad preterminal protein-dCMP initiation complex is discussed.

Adenoviridae↗
PubMed1988

Purification of a yeast protein that binds to origins of DNA replication and a transcriptional silencer.

Two factors that interact specifically with the chromosomal replicator, autonomously replicating sequence 1 (ARS1), were identified in whole-cell yeast extracts. One of these proteins, ARS binding factor I (ABF-I), was purified to homogeneity as a polypeptide of 135 kDa. ABF-I binds within a region previously shown to be essential for the function of ARS1 when yeast are grown under certain nutritional conditions, and deletion analysis presented here suggests that the ARS1 domain containing the ABF-I-binding site, domain B, is a complex element composed of at least two subdomains. ABF-I also binds within an ARS at the HMR silent mating locus. This ARS functions as a cis-acting transcriptional silencer, and the ABF-I-binding site within this ARS is important for both ARS and silencer function.

Base Sequence↗