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The DNA binding domain (POU domain) of transcription factor oct-1 suffices for stimulation of DNA replication.
- Source :
-
The EMBO journal [EMBO J] 1990 Jun; Vol. 9 (6), pp. 1883-8. - Publication Year :
- 1990
-
Abstract
- Oct-1, also referred to as NFIII, OTF-1, OBP100 or NF-A1, is a ubiquitous sequence-specific DNA binding protein that activates transcription and adenovirus DNA replication. The protein contains a conserved DNA binding domain (POU domain) present in several transcription factors. We have overproduced oct-1, the related oct-2 and several oct-1 deletion mutants in a vaccinia expression system to identify the domains important for activation of DNA replication in vitro. Both oct-1 and oct-2 stimulate adenovirus DNA replication in an octamer-dependent manner. From deletion studies it appears that the 160 amino acid long POU domain suffices for stimulation. This domain consists of two subdomains, a POU-specific and a homeo domain. Deletion of the POU-specific domain revealed that the homeo domain has an intrinsic, but weak DNA binding activity and surprisingly, inhibits DNA replication. As the POU domain does not coincide with the transcription activation domain, these results indicate that, although oct-1 functions both in DNA replication and transcription, the mechanisms underlying these processes are probably distinct.
- Subjects :
- Adenoviruses, Human growth & development
Base Sequence
DNA, Recombinant metabolism
DNA-Binding Proteins metabolism
Deoxyribonuclease I
HeLa Cells
Host Cell Factor C1
Humans
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Octamer Transcription Factor-1
Transcription Factors metabolism
Transfection
Virus Replication
Adenoviruses, Human genetics
DNA Replication
DNA, Viral metabolism
DNA-Binding Proteins genetics
Transcription Factors genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0261-4189
- Volume :
- 9
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- The EMBO journal
- Publication Type :
- Academic Journal
- Accession number :
- 2347308
- Full Text :
- https://doi.org/10.1002/j.1460-2075.1990.tb08314.x