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• W2287459411 abstract "Research Article15 November 1996 The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. R. J. Sarnovsky R. J. Sarnovsky Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author E. W. May E. W. May Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author N. L. Craig N. L. Craig Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author R. J. Sarnovsky R. J. Sarnovsky Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author E. W. May E. W. May Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author N. L. Craig N. L. Craig Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author Author Information R. J. Sarnovsky1, E. W. May1 and N. L. Craig1 1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. The EMBO Journal (1996)15:6348-6361https://doi.org/10.1002/j.1460-2075.1996.tb01024.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The bacterial transposon Tn7 translocates by a cut and paste mechanism: excision from the donor site results from double-strand breaks at each end of Tn7 and target insertion results from joining of the exposed 3′ Tn7 tips to the target DNA. Through site-directed mutagenesis of the Tn7-encoded transposition proteins TnsA and TnsB, we demonstrate that the Tn7 transposase is a heteromeric complex of these proteins, each protein executing different DNA processing reactions. TnsA mediates DNA cleavage reactions at the 5′ ends of Tn7, and TnsB mediates DNA breakage and joining reactions at the 3′ ends of Tn7. Thus the double-strand breaks that underlie Tn7 excision result from a collaboration between two active sites, one in TnsA and one in TnsB; the same (or a closely related) active site in TnsB also mediates the subsequent joining of the 3′ ends to the target. Both TnsA and TnsB appear to be members of the retroviral integrase superfamily: mutation of their putative DD(35)E motifs blocks catalytic activity. Recombinases of this class require a divalent metal cofactor that is thought to interact with these acidic residues. Through analysis of the metal ion specificity of a TnsA mutant containing a sulfur (cysteine) substitution, we provide evidence that a divalent metal actually interacts with these acidic amino acids. Next ArticlePrevious Article Volume 15Issue 221 November 1996In this issue RelatedDetailsLoading ..." @default.
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• W2287459411 date "1996-11-01" @default.
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• W2287459411 title "The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products." @default.
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• W2287459411 doi "https://doi.org/10.1002/j.1460-2075.1996.tb01024.x" @default.
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