Publications by authors named "Marie-Helene Hamelin"
The mariner Mos1 synaptic complex consists of a tetramer of transposase molecules that bring together the two ends of the element. Such an assembly requires at least two kinds of protein-protein interfaces. The first is involved in "cis" dimerization, and consists of transposase molecules bound side-by-side on a single DNA molecule.
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- The Mos1 transposable element's mobility relies on a synaptic complex, specifically the paired-end complex 2 (PEC2), formed by two inverted terminal repeats and a transposase tetramer.
- The assembly of PEC2 begins with a simpler single-end complex 2 (SEC2), which consists of one terminal repeat and two transposase molecules, showing a progression in complex formation.
- The study reveals two binding sites for transposase within one terminal repeat, highlighting a cooperative dimer formation that explains the interaction limitations of a single transposase with both the inverted repeat and target DNA.