tailieunhanh - Báo cáo khoa học: Leishmania donovani bisubunit topoisomerase I gene fusion leads to an active enzyme with conserved type IB enzyme function

All eukaryotic topoisomerase I enzymes are monomeric enzymes, whereas the kinetoplastid family (TrypanosomaandLeishmania) possess an unusual bisubunit topoisomerase I. To determine what happens to the enzyme architecture and catalytic property if the two subunits are fused, and to explore the functional relationship between the two subunits, we describe herein vitro gene fusion of Leishmaniabisubunit topoisomerase I into a single ORF encoding a new monomeric topoisomerase I (LdTOPIL-fus-S). | ễFEBS Journal Leishmania donovani bisubunit topoisomerase I gene fusion leads to an active enzyme with conserved type IB enzyme function Benu B. Das1 Somdeb Bose Dasgupta1 Agneyo Ganguly1 Saumyabrata Mazumder2 Amit Roy1 and Hemanta K. Majumder1 1 Department of Molecular Parasitology Indian Institute of ChemicalBiology Kolkata India 2 Infectious Diseases Group Indian Institute of ChemicalBiology Kolkata India Keywords camptothecin gene fusion Leishmania topoisomerase I SKXXY motif Correspondence H. K. Majumder Molecular Parasitology Laboratory Indian Institute of Chemical Biology 4 Raja . Mullick Road Kolkata-700032 India Fax 91 33 2473 5197 Tel 91 33 2412 3207 E-mail hkmajumder@ These authors contributed equally to this work Received 12 July 2006 revised 1 November 2006 accepted 6 November 2006 doi All eukaryotic topoisomerase I enzymes are monomeric enzymes whereas the kinetoplastid family Trypanosoma and Leishmania possess an unusual bisubunit topoisomerase I. To determine what happens to the enzyme architecture and catalytic property if the two subunits are fused and to explore the functional relationship between the two subunits we describe here in vitro gene fusion of Leishmania bisubunit topoisomerase I into a single ORF encoding a new monomeric topoisomerase I LdTOPIL-fus-S . It was found that LdTOPIL-fus-S is active. Gene fusion leads to a significant modulation of in vitro topoisomerase I activity compared to the wild-type heterodimeric enzyme LdTOPILS . Interestingly an N-terminal truncation mutant 1-210 amino acids of the small subunit when fused to the intact large subunit LdTOPIL-fus-A 1-210 S showed reduced topoisomerase I activity and camptothecin sensitivity in comparison to LdTOPIL-fus-S. Investigation of the reduction in enzyme activity indicated that the nonconserved 1-210 residues of LdTOPIS probably act as a pseudolinker domain between the core and catalytic domain of the fused Leishmania enzyme .

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