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A novel trafficking pathway in P lasmodium falciparum for the organellar localization of glutathione peroxidase‐like thioredoxin peroxidase
Author(s) -
Chaudhari Rahul,
Narayan Aishwarya,
Patankar Swati
Publication year - 2012
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2012.08746.x
Subject(s) - endoplasmic reticulum , golgi apparatus , brefeldin a , apicoplast , microbiology and biotechnology , biology , organelle , plasmodium falciparum , endomembrane system , secretory pathway , protein targeting , biochemistry , plastid , membrane protein , gene , chloroplast , membrane , malaria , immunology
Although common in plants, very few proteins are currently known to be localized to both the plastid and the mitochondrion in P lasmodium falciparum . One such protein is P . falciparum glutathione peroxidase‐like thioredoxin peroxidase ( P f TP x Gl ) which we show, by immunofluorescence imaging and bioinformatics predictions, is localized to the apicoplast, the mitochondrion and the cytosol. The distribution of P f TP x Gl was random in the population, with the protein localizing to any one organelle in some parasites and to both in others. It has been proposed that targeting to each organelle occurs via independent pathways that do not proceed via the Golgi. However, for P f TP x Gl , both incubation at low temperature (15 °C) and B refeldin A treatment reversibly blocked targeting to these organelles, suggesting the involvement of a novel trafficking route, most probably via the endoplasmic reticulum and G olgi. This idea is further supported by the lack of cleavage of the putative N ‐terminal signal sequence of P f TP x Gl , and this N ‐terminal extension did not compromise P f TP x Gl enzyme activity. In the context of evolution, a common pathway for the dual localization of a single gene product, such as the primitive endoplasmic reticulum– G olgi route, may have been retained as opposed to optimization for individual organellar import pathways.