Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway

被引:410
作者
Waller, RF [1 ]
Reed, MB
Cowman, AF
McFadden, GI
机构
[1] Univ Melbourne, Sch Bot, Plant Cell Biol Res Ctr, Parkville, Vic 3052, Australia
[2] Walter & Eliza Hall Inst Med Res, Parkville, Vic 3052, Australia
关键词
green fluorescent protein; malaria; plastid targeting; secretory pathway; transfection;
D O I
10.1093/emboj/19.8.1794
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The plastid of Plasmodium falciparum (or 'apicoplast') is the evolutionary homolog of the plant chloroplast and represents a vestige of a photosynthetic past. Apicoplast indispensability indicates that it still provides essential functions to parasites. Similar to plant chloroplasts, the apicoplast is dependent on many nucleus-encoded genes to provide these functions. The apicoplast is surrounded by four membranes, two more than plant chloroplasts. Thus, protein targeting to the apicoplast must overcome additional membrane barriers. In P.falciparum we have analyzed apicoplast targeting using green fluorescent protein (GFP). We demonstrate that protein targeting is at least a two-step process mediated by bipartite N-terminal presequences that consist of a signal peptide for entry into the secretory pathway and a plant-like transit peptide for subsequent import into the apicoplast. The P.falciparum transit peptide is exceptional compared with other known plastid transit peptides in not requiring serine or threonine residues. The presequence components are removed stepwise during apicoplast targeting. Targeting GFP to the apicoplast has also provided the first opportunity to examine apicoplast morphology in live P.falciparum.
引用
收藏
页码:1794 / 1802
页数:9
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