Control of simian virus 40 DNA replication by the HeLa cell nuclear kinase casein kinase I.
AUTOR(ES)
Cegielska, A
RESUMO
The initiation of simian virus 40 (SV40) DNA replication is regulated by the phosphorylation state of the viral initiator protein, large T antigen. We describe the purification from HeLa cell nuclei of a 35-kDa serine/threonine protein kinase that phosphorylates T antigen at sites that are phosphorylated in vivo and thereby inhibits its ability to initiate SV40 DNA replication. The inhibition of both origin unwinding and DNA replication by the kinase is reversed by protein phosphatase 2A. As determined by molecular weight, substrate specificity, autophosphorylation, immunoreactivity, and limited sequence analysis, this kinase appears to be identical to casein kinase I, a ubiquitous serine/threonine protein kinase that is closely related to a yeast kinase involved in DNA metabolism. The HeLa cell phosphorylation cycle that controls the initiation of SV40 DNA replication may also play a role in cellular DNA metabolism.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=359005Documentos Relacionados
- Assembly of nascent DNA into nucleosome structures in simian virus 40 chromosomes by HeLa cell extract.
- Accurate transcription of simian virus 40 chromatin in a HeLa cell extract.
- Vaccinia virus infection of HeLa cells. I. Synthesis of vaccinia DNA in host cell nuclei.
- Breakdown of HeLa Cell DNA Mediated by Vaccinia Virus
- Transcription of Simian Virus 40 chromosomes in an extract of HeLa cells.
