Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Chauhan, Manish; Tuteja, Renu

doi:10.1038/s41598-018-38032-1

Cited by 5 publications

(10 citation statements)

References 66 publications

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“…It can unwind DNA in both the 3′–5′ and 5′–3′ directions. Its dual and bipolar helicase activities are similar to other previously characterized helicases present in P. falciparum such as PfDH60, PfH45, and PfPSH2 . PfPSH1 shows similar activities to PfPSH2 as both are dual and bipolar helicases.…”

Section: Discussionsupporting

confidence: 70%

“…The subcellular localization of PfPSH1 was studied with the help of immunofluorescence microscopy, and it is majorly present in the cytoplasm and partially in the nucleus of the parasite in all the intraerythrocytic developmental stages. It has been previously reported that PfPSH2 and PfPSH3 are localized in both nucleus and cytoplasm in intraerythrocytic developmental stages .…”

Section: Discussionmentioning

confidence: 95%

“…PfPSH1CM shows loss in ATPase activity, and similarly, helicase activity of the mutant was also abrogated. PfPSH1 is unique in requirement of nucleotide triphosphate when compared to other PSHs (PfPSH2 and PfPSH3); it prefers CTP more than UTP and ATP to unwind DNA, whereas PfPSH2 and PfPSH3 prefer only ATP [19,20]. Despite having similar core and signature motifs various helicases behave differently, previous reports suggest that PfWrn prefers GTP than ATP to unwind DNA and PfUvrD has no preference, and it can unwind well with all four NTPs [32,35].…”

Section: Discussionmentioning

confidence: 96%

“…PfPSH2 has bipolar direction specificity, but PfPSH3 exhibits only 3 0 -5 0 direction-specific activity. The localization studies suggest that PfPSH2 is mainly localized in the cytoplasm, but the localization of PfPSH3 is nucleocytoplasmic [19,20].…”

mentioning

confidence: 99%

“…Our previous studies have shown that there are three parasite‐specific helicases (PSH) present in P. falciparum . In recent studies, we have reported the detailed characterization of two PSH (PfPSH2 and PfPSH3) . The biochemical characterization shows that both PfPSH2 and PfPSH3 are DNA‐dependent ATPases, whereas PfPSH2 also shows RNA‐dependent ATPase activity.…”

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confidence: 99%

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Biochemical characterization of Plasmodium falciparum parasite specific helicase 1 (PfPSH1)

et al. 2019

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Malaria, a disease caused by infection with parasites of the genus Plasmodium, causes millions of deaths worldwide annually. Of the five Plasmodium species that can infect humans, Plasmodium falciparum causes the most serious parasitic infection. The emergence of drug resistance and the ineffectiveness of old therapeutic regimes against malaria mean there is an urgent need to better understand the basic biology of the malaria parasite. Previously, we have reported the presence of parasite‐specific helicases identified through genome‐wide analysis of the P. falciparum (3D7) strain. Helicases are involved in various biological pathways in addition to nucleic acid metabolism, making them an important target of study. Here, we report the detailed biochemical characterization of P. falciparum parasite‐specific helicase 1 (PfPSH1) and the effect of phosphorylation on its biochemical activities. The C‐terminal of PfPSH1 (PfPSH1C) containing all conserved domains was used for biochemical characterization. PfPSH1C exhibits DNA‐ or ribonucleic acid (RNA)‐stimulated ATPase activity, and it can unwind DNA and RNA duplex substrates. It shows bipolar directionality because it can translocate in both (3′–5′ and 5′–3′) directions. PfPSH1 is mainly localized to the cytoplasm during early stages (including ring and trophozoite stages of intraerythrocytic development), but at late stages, it is partially located in the cytoplasm. The biochemical activities of PfPSH1 are upregulated after phosphorylation with PKC. The detailed biochemical characterization of PfPSH1 will help us understand its functional role in the parasite and pave the way for future studies.

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Section: Discussionsupporting

confidence: 70%

Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

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confidence: 99%

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Biochemical characterization of Plasmodium falciparum parasite specific helicase 1 (PfPSH1)

et al. 2019

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Plasmodium falciparum DDX17 is an RNA helicase crucial for parasite development

Sourabh

Chauhan

Yasmin

et al. 2021

Biochemistry and Biophysics Reports

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Malaria is one of the major global health concerns still prevailing in this 21st century. Even the effect of artemisinin combination therapies (ACT) have declined and causing more mortality across the globe. Therefore, it is important to understand the basic biology of malaria parasite in order to find novel drug targets. Helicases play important role in nucleic acid metabolism and are components of cellular machinery in various organisms. In this manuscript we have performed the biochemical characterization of homologue of DDX17 from Plasmodium falciparum (PfDDX17). Our results show that PfDDX17 is an active RNA helicase and uses mostly ATP for its function. The qRT-PCR experiment results suggest that PfDDX17 is highly expressed in the trophozoite stage and it is localised mainly in the cytoplasm and in infected RBC (iRBC) membrane mostly in the trophozoite stage. The dsRNA knockdown study suggests that PfDDX17 is important for cell cycle progression. These studies report the biochemical functions of PfDDX17 helicase and further augment the fundamental knowledge about helicase families of P. falciparum .

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Plasmodium falciparum DDX31 is DNA helicase localized in nucleolus

Yasmin

Chauhan

Sourabh

et al. 2019

Heliyon

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Malaria is a major infectious disease and is responsible for millions of infections every year. As drug resistance strains of Plasmodium species are emerging, there is an urgent need to understand the parasite biology and identify new drug targets. Helicases are very important enzymes that participate in various nucleic acid metabolic processes. Previously we have reported several putative DEAD box helicases in the genome of Plasmodium falciparum 3D7 strain. In this study, we present biochemical characterization of one of the members of Has1 (Helicase associated with SET1) family of DEAD box proteins from P. falciparum 3D7 strain. PfDDX31 is a homologue of human DDX31 helicase and contains all the conserved characteristics motifs. The core PfDDX31C exhibits DNA and RNA dependent ATPase activity and unwinds partially duplex DNA by utilizing ATP or dATP only. The immunofluorescence assay results show that PfDDX31 is expressed throughout all the intraerythrocytic developmental stages in P. falciparum 3D7 strain. The co-localization with nucleolar marker PfNop1 further suggests that PfDDX31 is mostly present in nucleolus, a discrete nuclear compartment.

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Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Cited by 5 publications

References 66 publications

Biochemical characterization of Plasmodium falciparum parasite specific helicase 1 (PfPSH1)

Biochemical characterization of Plasmodium falciparum parasite specific helicase 1 (PfPSH1)

Plasmodium falciparum DDX17 is an RNA helicase crucial for parasite development

Plasmodium falciparum DDX31 is DNA helicase localized in nucleolus

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