Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.

Apicoplasts are vestigial plastids in apicomplexan parasites like Plasmodium, the causative agent of malaria. Apicomplexan parasites are dependant on their apicoplasts for synthesis of various molecules that they are unable to scavenge in sufficient quantity from their host, which makes apicoplasts...

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Main Authors: Liting Lim, Claire P Sayers, Christopher D Goodman, Geoffrey I McFadden
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2016-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4956234?pdf=render
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spelling doaj-48cb794185054eea99dfb676a876fe8c2020-11-25T02:47:03ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01117e015960310.1371/journal.pone.0159603Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.Liting LimClaire P SayersChristopher D GoodmanGeoffrey I McFaddenApicoplasts are vestigial plastids in apicomplexan parasites like Plasmodium, the causative agent of malaria. Apicomplexan parasites are dependant on their apicoplasts for synthesis of various molecules that they are unable to scavenge in sufficient quantity from their host, which makes apicoplasts attractive drug targets. Proteins known as plastid phosphate translocators (pPTs) are embedded in the outer apicoplast membrane and are responsible for the import of carbon, energy and reducing power to drive anabolic synthesis in the organelle. We investigated how a pPT is targeted into the outer apicoplast membrane of the human malaria parasite P. falciparum. We showed that a transmembrane domain is likely to act as a recessed signal anchor to direct the protein into the endomembrane system, and that a tyrosine in the cytosolic N-terminus of the protein is essential for targeting, but one or more, as yet unidentified, factors are also essential to direct the protein into the outer apicoplast membrane.http://europepmc.org/articles/PMC4956234?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Liting Lim
Claire P Sayers
Christopher D Goodman
Geoffrey I McFadden
spellingShingle Liting Lim
Claire P Sayers
Christopher D Goodman
Geoffrey I McFadden
Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
PLoS ONE
author_facet Liting Lim
Claire P Sayers
Christopher D Goodman
Geoffrey I McFadden
author_sort Liting Lim
title Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
title_short Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
title_full Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
title_fullStr Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
title_full_unstemmed Targeting of a Transporter to the Outer Apicoplast Membrane in the Human Malaria Parasite Plasmodium falciparum.
title_sort targeting of a transporter to the outer apicoplast membrane in the human malaria parasite plasmodium falciparum.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2016-01-01
description Apicoplasts are vestigial plastids in apicomplexan parasites like Plasmodium, the causative agent of malaria. Apicomplexan parasites are dependant on their apicoplasts for synthesis of various molecules that they are unable to scavenge in sufficient quantity from their host, which makes apicoplasts attractive drug targets. Proteins known as plastid phosphate translocators (pPTs) are embedded in the outer apicoplast membrane and are responsible for the import of carbon, energy and reducing power to drive anabolic synthesis in the organelle. We investigated how a pPT is targeted into the outer apicoplast membrane of the human malaria parasite P. falciparum. We showed that a transmembrane domain is likely to act as a recessed signal anchor to direct the protein into the endomembrane system, and that a tyrosine in the cytosolic N-terminus of the protein is essential for targeting, but one or more, as yet unidentified, factors are also essential to direct the protein into the outer apicoplast membrane.
url http://europepmc.org/articles/PMC4956234?pdf=render
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AT clairepsayers targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum
AT christopherdgoodman targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum
AT geoffreyimcfadden targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum
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