Tn7 transposition: target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 8384534.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
We have reconstituted the transposition of the bacterial transposon Tn7 into its specific insertion site attTn7 with four purified Tn7-encoded proteins, TnsA+TnsB+TnsC+TnsD, and ATP. TnsA+TnsB+TnsC form a "core" recombination machine that recognizes the transposon ends and executes DNA breakage and joining; TnsD specifically recognizes attTn7. TnsA+TnsB+TnsC are specifically targeted to attTn7 through the TnsD-dependent interaction of TnsC, a nonspecific DNA-binding protein, with attTn7. Recombination appears to be activated by the assembly of a nucleoprotein complex containing the DNA substrates and Tns proteins. We suggest that TnsC plays a central role in communication between the transposon and the target DNA, particularly in directing insertion away from DNAs already containing a copy of Tn7.
Medical subject headings
- Bacterial Proteins
- DNA Transposable Elements
- DNA, Bacterial
- DNA-Binding Proteins
- Recombination, Genetic