Interaction of the DNA untwisting enzyme with the SV40 nucleoprotein complex.
AUTOR(ES)
Young, L S
RESUMO
The SV40 nucleoprotein complex which was isolated from infected CV-1 cells did not possess an active DNA untwisting enzyme. The superhelix density of the DNA in the chromatin complex was unchanged after treatment with purified rat liver DNA untwisting enzyme. However, in the presence of ethidium bromide (1 microgram/ml) the superhelix density was changed. Moreover, the nicked intermediate in the DNA untwisting reaction could be detected using the chromatin DNA as a substrate. These results show that the DNA in the SV40 chromatin which is accessible to the DNA untwisting enzyme is under no topological strain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=342007Documentos Relacionados
- The sv40 transcription complex. II. Non-dissociation of protein from SV40 chromatin during transcription.
- Nicking-closing enzyme is associated with SV40 DNA in vivo as a sodium dodecyl sulfate-resistant complex.
- DNA polymerase alpha is associated with replicating SV40 nucleoprotein complexes.
- Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication.
- In situ nucleoprotein structure involving origin-proximal SV40 DNA control elements.