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- W123038640 abstract "Research Article20 December 1988free access VirD proteins of Agrobacterium tumefaciens are required for the formation of a covalent DNA–protein complex at the 5′ terminus of T-strand molecules. A. Herrera-Estrella A. Herrera-Estrella Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author Z. M. Chen Z. M. Chen Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author M. Van Montagu M. Van Montagu Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author K. Wang K. Wang Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author A. Herrera-Estrella A. Herrera-Estrella Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author Z. M. Chen Z. M. Chen Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author M. Van Montagu M. Van Montagu Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author K. Wang K. Wang Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. Search for more papers by this author Author Information A. Herrera-Estrella1, Z. M. Chen1, M. Van Montagu1 and K. Wang1 1Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. The EMBO Journal (1988)7:4055-4062https://doi.org/10.1002/j.1460-2075.1988.tb03299.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The T-DNA transfer process of Agrobacterium tumefaciens is activated by the induction of the Ti plasmid virulence (vir) loci by plant signal molecules such as acetosyringone. Upon initiation of the T-DNA transfer process, site-specific nicks occur at the 25-bp border sequences. This cleavage leads to the generation of a free, linear ssT-DNA molecule which is bound by sequence non-specific VirE proteins. Here we present evidence for the involvement of other acetosyringone-induced proteins in the formation of a covalent complex between the T-strand and protein, designated the T-complex. Alkaline gel-electrophoretic analysis showed that proteins specifically bind to the 5′ termini of nicked T-DNA molecules. The T-complex can be formed in Escherichia coli when the VirD1 and VirD2 proteins are expressed. Previous ArticleNext Article Volume 7Issue 131 December 1988In this issue RelatedDetailsLoading ..." @default.
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- W123038640 title "VirD proteins of Agrobacterium tumefaciens are required for the formation of a covalent DNA-protein complex at the 5′ terminus of T-strand molecules." @default.
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