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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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 |
work_keys_str_mv |
AT litinglim targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum AT clairepsayers targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum AT christopherdgoodman targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum AT geoffreyimcfadden targetingofatransportertotheouterapicoplastmembraneinthehumanmalariaparasiteplasmodiumfalciparum |
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