AI Article Synopsis
- Helicases help open up DNA and RNA structures and are vital for various cellular processes involving these molecules.
- Researchers have cloned and studied a DEAD box helicase from the malaria parasite Plasmodium falciparum, revealing it shares similarities with a yeast protein named Has1p.
- This helicase can unwind nucleic acids using different types of nucleotide triphosphates and its activity heavily relies on a specific part of its structure known as the N-terminal region, in addition to a conserved helicase domain.
Article Abstract
Helicases catalyze the opening of nucleic acid duplexes and are implicated in many nucleic acid metabolic cellular processes that require single stranded DNA or reorganization of RNA structure. Previously we have reported that Plasmodium falciparum genome contains a number of DEAD box helicases. In the present study we report the cloning, expression and characterization of one of the novel members of DEAD box family from P. falciparum. Our results indicate that it is a homologue of Has1p from yeast and it contains DNA and RNA unwinding, nucleic acid-dependent ATPase and RNA binding activities. This enzyme can utilize all the nucleosidetriphosphates (NTPs) and deoxy nucleosidetriphosphates (dNTPs) for its unwinding activity. Using a truncated derivative of this protein we further report that the N-terminal region of the protein is essentially required for its activity. These studies suggest that besides the conserved helicase domain the highly variable N-terminal region also contributes in the activity of the protein.
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| http://dx.doi.org/10.1016/j.parint.2010.02.003 | DOI Listing |
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