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• W1528256607 abstract "Research Article1 February 1990free access Amino-terminal domain of NF1 binds to DNA as a dimer and activates adenovirus DNA replication. F. Gounari F. Gounari European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. De Francesco R. De Francesco European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author J. Schmitt J. Schmitt European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author P. van der Vliet P. van der Vliet European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. Cortese R. Cortese European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author H. Stunnenberg H. Stunnenberg European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author F. Gounari F. Gounari European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. De Francesco R. De Francesco European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author J. Schmitt J. Schmitt European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author P. van der Vliet P. van der Vliet European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author R. Cortese R. Cortese European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author H. Stunnenberg H. Stunnenberg European Molecular Biology Laboratory, Heidelberg, FRG. Search for more papers by this author Author Information F. Gounari1, R. De Francesco1, J. Schmitt1, P. Vliet1, R. Cortese1 and H. Stunnenberg1 1European Molecular Biology Laboratory, Heidelberg, FRG. The EMBO Journal (1990)9:559-566https://doi.org/10.1002/j.1460-2075.1990.tb08143.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info NF1 is a DNA-binding protein involved in initiation of adenovirus DNA replication as well as in modulating the rate of transcription initiation of genes containing the sequence TGGCA. We show here that recombinant NF1 expressed via vaccinia virus is transported into the nucleus and binds to its cognate sequences with the same specificity as NF1 purified from HeLa cells. Furthermore, the recombinant NF1 forms oligomers in solution and binds as a dimer to palindromic as well as half-site sequences. NF1 expressed via vaccinia virus stimulates the initiation of adenovirus replication in vitro. The N-terminal 240 amino acids of the protein are sufficient for full DNA-binding activity as well as stimulation of adenovirus replication. By analysis of several NF1 mutants translated in vitro, we also define the minimal DNA-binding domain and localize the region responsible for DNA binding on the N-terminal and for oligomerization on the C-terminal side of this domain. Previous ArticleNext Article Volume 9Issue 21 February 1990In this issue RelatedDetailsLoading ..." @default.
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• W1528256607 title "Amino-terminal domain of NF1 binds to DNA as a dimer and activates adenovirus DNA replication." @default.
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