Topic
Nuclear factor I
About: Nuclear factor I is a research topic. Over the lifetime, 244 publications have been published within this topic receiving 14988 citations. The topic is also known as: CTF/NFI & IPR000647.
Papers published on a yearly basis
Papers
TL;DR: It is concluded that CTF/NF-I can serve both as a transcription selectivity factor for RNA polymerase II and as an initiation factor for adenovirus DNA replication.
987 citations
TL;DR: Human CTF/NF-I consists of a family of CCAAT box binding proteins that activate both transcription and DNA replication and analysis of cDNA mutants reveals that the N-terminal portion of CTF-1 is sufficient for site-specific DNA recognition, protein dimerization, and adenovirus replication.
791 citations
TL;DR: A family of related multisubunit CCAAT-binding proteins that are composed of heterologous subunits are proposed that are related to each other and to the adenovirus origin of replication and is required for the initiation ofadenoviral replication.
665 citations
TL;DR: The promoter of the mouse albumin gene contains at least six binding sites for specific DNA-binding proteins (A to F), and both of these competing binding sites are required for maximal in vitro transcription.
491 citations
TL;DR: It is suggested that the initiation reaction observed with Ad DNA-prot in the absence of Ad DBP occurs at single-stranded DNA sites, creating a requirement for nuclear factor I in pTP-dCMP complex formation.
Abstract: A protein factor that participates in the formation of a covalent complex between the 80,000-dalton precursor of the adenovirus (Ad) terminal protein (pTP) and 5'-dCMP has been isolated and characterized. This 47,000-dalton protein, isolated from nuclear extracts of uninfected HeLa cells, has been designated nuclear factor I. It is free of detectable DNA polymerase alpha, beta, and gamma activities. In the presence of Ad DNA-prot, the Ad-protein fraction (containing the pTP and the Ad-associated DNA polymerase), ATP, Mg2+, and dCTP, nuclear factor I stimulates formation of the pTP-dCMP complex. Addition of the Ad DNA binding protein (Ad DBP) renders the formation of the pTP-dCMP complex completely dependent on the addition of nuclear factor I. When Ad DNA-prot is replaced with phi X174 single-stranded circular DNA, pTP-dCMP complex formation requires only the Ad-protein fraction; Ad DBP and ATP are inhibitory and nuclear factor I has no effect on this reaction. This suggests that the initiation reaction observed with Ad DNA-prot in the absence of Ad DBP occurs at single-stranded DNA sites. In the presence of Ad DBP, these sites are blocked thus creating a requirement for nuclear factor I in pTP-dCMP complex formation.
357 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2020 | 2 |
| 2019 | 2 |
| 2018 | 3 |
| 2017 | 3 |
| 2016 | 2 |
| 2015 | 4 |