Tn7 transposition: target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system
Article Abstract:
A study of the mechanism of transposition of the bacterial DNA Tn7, which shows a high degree of target site selectivity during transposition, is reported. Critical transposition steps include the selection of an insertion site, breakage from donor DNA and joining with the target DNA. The four Tn7-encoded proteins TnsA+TnsB+TnsC+TnsD and ATP were shown to be essential for the transposition of Tn7 into its specific insertion site attTn7. The individual and combined functions of the Tn7-encoded proteins are discussed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site
Article Abstract:
A single active site has been theorized to catalyze the three chemical steps involved in the non-replicative transposition of transposon-transposase protein Tn10/IS10 complex. The single active site was determined after studies of four tranposase mutations showed an intact synaptic complex even with the deletion of a chemical step. A single transposase monomer at each end of the DNA catalyzes the cleavage of two strands, with the strand transfer catalyzed by the same monomer that catalyzed the cleavage.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Quality control in Mu DNA transposition
Article Abstract:
Nucleoprotein architecture plays an important role in initiating Mu DNA transposition. Mu transposition occurs in trans, with transposase bound to sites located at each end of the Mu genome. Transposition is initiated by cleavage at the 3' ends of the transposon and a transesterification reaction splices these ends into a target DNA. Mu transposition also utilizes nucleoprotein architecture as a regulatory mechanism.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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