| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1179172 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2016 | 15 Pages |
Abstract
Malaria caused by Plasmodium, particularly Plasmodium falciparum, is the most serious and widespread parasitic disease of humans. RecQ helicases present in each organism differ and several homologues have been identified in various multicellular organisms. In the present study we report the detailed biochemical and functional characterization of the Bloom (Blm) homologue (PfBlm) from P. falciparum 3D7 strain. Purified PfBlm exhibits ATPase and 3â² to 5â² direction specific DNA helicase activity. Immunofluorescence assay results show that PfBlm is expressed in all the stages of intraerythrocytic development of the P. falciparum 3D7 strain and in addition to nucleus in some stages of development it localizes in the cytoplasm also.226
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Authors
Farhana Rahman, Mohammed Tarique, Renu Tuteja,