Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction

Abstract Plasmodium falciparum is responsible for most dangerous and prevalent form of malaria. The emergence of multi drug resistant parasite hindered the prevention of malaria burden worldwide. Helicases are omnipresent enzymes, which play important role in nucleic acid metabolism and can be used...

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Autores principales:	Manish Chauhan, Mohammed Tarique, Renu Tuteja
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ef235fd7fc1643a590b3f5aaede84fde
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spelling	oai:doaj.org-article:ef235fd7fc1643a590b3f5aaede84fde2021-12-02T15:04:55ZPlasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction10.1038/s41598-017-12927-x2045-2322https://doaj.org/article/ef235fd7fc1643a590b3f5aaede84fde2017-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-12927-xhttps://doaj.org/toc/2045-2322Abstract Plasmodium falciparum is responsible for most dangerous and prevalent form of malaria. The emergence of multi drug resistant parasite hindered the prevention of malaria burden worldwide. Helicases are omnipresent enzymes, which play important role in nucleic acid metabolism and can be used as potential targets for development of novel therapeutics. The genome wide analysis of P. falciparum 3D7 strain revealed some novel parasite specific helicases, which are not present in human host. Here we report the detailed biochemical characterization of P. falciparum parasite specific helicase 3 (PfPSH3). The characteristic ATPase and helicase activities of PfPSH3 reside in its N-terminal region (PfPSH3N) as it contains all the conserved signature motifs whereas the C-terminal does not show any detectable biochemical activity. PfPSH3N also shows DNA helicase activity in the 3′–5′ direction. The immunofluorescence microscopy results show that PSH3 is localized in nucleus as well as in cytoplasm during different stages such as trophozoite and early schizont stages of intraerythrocytic development. This report sets the foundation for further study of parasite specific helicases and will be helpful in understanding the parasite biology.Manish ChauhanMohammed TariqueRenu TutejaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Manish Chauhan Mohammed Tarique Renu Tuteja Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
description	Abstract Plasmodium falciparum is responsible for most dangerous and prevalent form of malaria. The emergence of multi drug resistant parasite hindered the prevention of malaria burden worldwide. Helicases are omnipresent enzymes, which play important role in nucleic acid metabolism and can be used as potential targets for development of novel therapeutics. The genome wide analysis of P. falciparum 3D7 strain revealed some novel parasite specific helicases, which are not present in human host. Here we report the detailed biochemical characterization of P. falciparum parasite specific helicase 3 (PfPSH3). The characteristic ATPase and helicase activities of PfPSH3 reside in its N-terminal region (PfPSH3N) as it contains all the conserved signature motifs whereas the C-terminal does not show any detectable biochemical activity. PfPSH3N also shows DNA helicase activity in the 3′–5′ direction. The immunofluorescence microscopy results show that PSH3 is localized in nucleus as well as in cytoplasm during different stages such as trophozoite and early schizont stages of intraerythrocytic development. This report sets the foundation for further study of parasite specific helicases and will be helpful in understanding the parasite biology.
format	article
author	Manish Chauhan Mohammed Tarique Renu Tuteja
author_facet	Manish Chauhan Mohammed Tarique Renu Tuteja
author_sort	Manish Chauhan
title	Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
title_short	Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
title_full	Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
title_fullStr	Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
title_full_unstemmed	Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction
title_sort	plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds dna duplex in 3′ to 5′ direction
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ef235fd7fc1643a590b3f5aaede84fde
work_keys_str_mv	AT manishchauhan plasmodiumfalciparumspecifichelicase3isnucleocytoplasmicproteinandunwindsdnaduplexin3to5direction AT mohammedtarique plasmodiumfalciparumspecifichelicase3isnucleocytoplasmicproteinandunwindsdnaduplexin3to5direction AT renututeja plasmodiumfalciparumspecifichelicase3isnucleocytoplasmicproteinandunwindsdnaduplexin3to5direction
_version_	1718388991402704896

Plasmodium falciparum specific helicase 3 is nucleocytoplasmic protein and unwinds DNA duplex in 3′ to 5′ direction

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