Author/Authors :
Dasari , Jagadish Babu Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Soren , Bini Chhetri Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Ottaviani , Alessio Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Tesauro , Cinzia Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Marino , Simona Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Messina , Beatrice Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy , Fiorani , Paola Department of Biology - University of Rome Tor Vergata - Via Della Ricerca Scientifica 1- 00133 Rome, Italy
Abstract :
DNA topoisomerases 1B are a class of ubiquitous enzyme that solves the topological problems
associated with biological processes such as replication, transcription and recombination. Numerous sequence
alignment of topoisomerase 1B from different species shows that the lengths of different domains as well as
their amino acids sequences are quite different. In the present study a hybrid enzyme, generated by swapping
the N-terminal of Plasmodium falciparum into the corresponding domain of the human, has been
characterized.
Methods: The chimeric enzyme was generated using different sets of PCR. The in vitro characterization was
carried out using different DNA substrate including radio-labelled oligonucleotides.
Results: The chimeric enzyme displayed slower relaxation activity, cleavage and re-ligation kinetics strongly
perturbed when compared to the human enzyme.
Conclusions: These results indicate that the N-terminal domain has a crucial role in modulating topoisomerase
activity in different species.
