Nucleic Acids Research, Vol 27, Issue 13 2745-2752, Copyright © 1999 by Oxford University Press
S Broccoli, JF Marquis, B Papadopoulou, M Olivier and M Drolet
In order to clone the gene encoding a type I DNA topoisomerase from
Leishmania donovani, a PCR-amplified DNA fragment obtained with degenerate
oligodeoxyribonucleotides was used to screen a genomic library from this
parasite. An open reading frame of 1905 bases encoding a putative protein
of 635 amino acid residues was isolated. A substantial part of the protein
shares a significant degree of homology with the sequence of other known
members of the IB topoisomerase family, in a highly conserved region of
these enzymes termed the core domain. However, homology is completely lost
after this conserved central core. Moreover, no conventional active
tyrosine site could be identified. In fact, the protein expressed in
Escherichia coli did not show any relaxation activity in vitro and was
unable to complement a mutant deficient in topoisomerase I activity. The
results of Southern blot experiments strongly suggested that the cloned
gene was not a pseudogene. Northern analysis revealed that the gene was
transcribed in its full length and also excluded the possibility that some
form of splicing is necessary to produce a mature messenger. Furthermore,
our results indicate that the gene is preferentially expressed in actively
growing L.donovani promastigotes and that it is also expressed in other
kinetoplastid parasites.
ARTICLES
Characterization of a Leishmania donovani gene encoding a protein that closely resembles a type IB topoisomerase
Departement de Microbiologie et Immunologie, Universite de Montreal, CP 6128, Succursale Centre-Ville, Montreal, Quebec H3C 3J7, Canada and.
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