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Falcilysin and its role in transit p...

Ponpuak, Marisa.

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Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast./
Author:	Ponpuak, Marisa.
Description:	141 p.
Notes:	Adviser: Daniel E. Goldberg.
Contained By:	Dissertation Abstracts International68-06B.
Subject:	Biology, Parasitology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3268078
ISBN:	9780549072119

Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast.
Ponpuak, Marisa.

Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast. - 141 p.

Adviser: Daniel E. Goldberg.

Thesis (Ph.D.)--Washington University in St. Louis, 2007.

Falcilysin (FLN) is an M16 zinc metalloprotease previously shown to function in the hemoglobin degradation pathway of the human malaria parasite Plasmodium falciparum. Hemoglobin degradation is an essential metabolic process that occurs in a specialized organelle called the acidic food vacuole. Two different classes of enzymes, aspartic proteases (plasmepsins) and cysteine proteases (falcipains), have been shown to initiate the hemoglobin cleavage. Generated peptide products are then further digested by FLN. In support of its role within the food vacuole, FLN has been shown to be located in this organelle. In addition, FLN has additional distribution outside the food vacuole. Since FLN can function very well at both acidic and neutral pH, an additional extravacuolar role has been proposed for this enzyme. This thesis aimed to characterize the neutral pH function of FLN. Using a transgenic parasite clone expressing a chromosomally encoded FLN-GFP fusion to determine its cellular locations, FLN was found to accumulate in an essential chloroplast-like organelle termed the apicoplast. Nuclear encoded proteins are targeted to the organelle by a bipartite N-terminal sequence comprised of a signal peptide followed by a positively charged transit peptide domain. The signal peptide is presumably cleaved off during cotranslational import into the ER. The transit peptide then directs the preproteins into the apicoplast stroma where it is cleaved off to release the mature proteins. Free transit peptides are believed to be harmful to the plastids and need to be rapidly destroyed. Evidence is provided that FLN participates in transit peptide degradation based on its ability to degrade transit peptides once liberated from preprotein and based on its grouping with PrePs, enzymes shown to be responsible for free transit peptide degradation in plant chloroplasts. The inability to chromosomally disrupt the FLN gene locus in cultured parasites suggests strongly that FLN is important for parasite development and hence an attractive antimalarial target.

ISBN: 9780549072119Subjects--Topical Terms:

1028974
Biology, Parasitology.

Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast.
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100 1 $a Ponpuak, Marisa. $3 1267719
245 1 0 $a Falcilysin and its role in transit peptide degradation in the Plasmodium falciparum apicoplast.
300 $a 141 p.
500 $a Adviser: Daniel E. Goldberg.
500 $a Source: Dissertation Abstracts International, Volume: 68-06, Section: B, page: 3602.
502 $a Thesis (Ph.D.)--Washington University in St. Louis, 2007.
520 $a Falcilysin (FLN) is an M16 zinc metalloprotease previously shown to function in the hemoglobin degradation pathway of the human malaria parasite Plasmodium falciparum. Hemoglobin degradation is an essential metabolic process that occurs in a specialized organelle called the acidic food vacuole. Two different classes of enzymes, aspartic proteases (plasmepsins) and cysteine proteases (falcipains), have been shown to initiate the hemoglobin cleavage. Generated peptide products are then further digested by FLN. In support of its role within the food vacuole, FLN has been shown to be located in this organelle. In addition, FLN has additional distribution outside the food vacuole. Since FLN can function very well at both acidic and neutral pH, an additional extravacuolar role has been proposed for this enzyme. This thesis aimed to characterize the neutral pH function of FLN. Using a transgenic parasite clone expressing a chromosomally encoded FLN-GFP fusion to determine its cellular locations, FLN was found to accumulate in an essential chloroplast-like organelle termed the apicoplast. Nuclear encoded proteins are targeted to the organelle by a bipartite N-terminal sequence comprised of a signal peptide followed by a positively charged transit peptide domain. The signal peptide is presumably cleaved off during cotranslational import into the ER. The transit peptide then directs the preproteins into the apicoplast stroma where it is cleaved off to release the mature proteins. Free transit peptides are believed to be harmful to the plastids and need to be rapidly destroyed. Evidence is provided that FLN participates in transit peptide degradation based on its ability to degrade transit peptides once liberated from preprotein and based on its grouping with PrePs, enzymes shown to be responsible for free transit peptide degradation in plant chloroplasts. The inability to chromosomally disrupt the FLN gene locus in cultured parasites suggests strongly that FLN is important for parasite development and hence an attractive antimalarial target.
590 $a School code: 0252.
650 4 $a Biology, Parasitology. $3 1028974
690 $a 0718
710 2 $a Washington University in St. Louis. $3 1017519
773 0 $t Dissertation Abstracts International $g 68-06B.
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