Production of simian virus 40 large tumor antigen in bacteria: Altered DNA-binding specificity and DNA-replication activity of underphosphorylated large tumor antigen

I. J. Mohr, Y. Gluzman, M. P. Fairman, M. Strauss, D. McVey, B. Stillman, R. D. Gerard

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

A bacterial expression system was used to produce simian virus 40 large tumor antigen (T antigen) in the absence of the extensive posttranslational modifications that occur in mammalian cells. Wild-type T antigen produced in bacteria retained a specific subset of the biochemical activities displayed by its mammalian counterpart. Escherichia coli T antigen functioned as a helicase and bound to DNA fragments containing either site I or the wild-type origin of replication in a manner identical to mammalian T antigen. However, T antigen purified from E. coli did not efficiently bind to site II, an essential cis element within simian virus 40 origin of replication. It therefore could not unwind origin-containing plasmids or efficiently replicate simian virus 40 DNA in vitro. The ability of protein phosphorylation to modulate the intrinsic preference of full-length T antigen for either site I or site II is discussed.

Original languageEnglish (US)
Pages (from-to)6479-6483
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number17
DOIs
StatePublished - 1989

ASJC Scopus subject areas

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