文章基本信息

标题：Replication of adenovirus DNA-protein complex with purified proteins
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作者：J E Ikeda ; T Enomoto ; J Hurwitz 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：2
页码：884-888
DOI：10.1073/pnas.78.2.884
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A protein fraction isolated from the cytosol of adenovirus-infected HeLa cells, which contained DNA polymerase alpha, catalyzed adenoviral DNA replication in the presence of adenovirus DNA binding protein, eukaryotic DNA polymerase beta, ATP, all four dNTPs, and MgCl2. DNA replication started at either end of exogenously added adenoviral DNA and was totally dependent on the presence of terminal 55,000-dalton proteins on the DNA template. The replicaton of adenovirus DNA in the system was sensitive to aphidicolin and retained nearly all the properties of DNA replication that occur in vivo or in vitro with crude extracts. The 5'-ends of the newly synthesized adenovirus DNA strands were covalently linked to an 80,000-dalton protein linked to dCMP. DNA synthesized with purified proteins was only 25-50+ the length of parental viral strands. Addition of cytosol extracts from uninfected HeLa cells to reaction mixtures containing purified proteins gave full-length adenoviral DNA strands.