A thioredoxin family protein of the apicoplast periphery identifies abundant candidate transport vesicles in Toxoplasma gondii

被引：73

作者：

DeRocher, Amy E. ^{[1
]}

Coppens, Isabelle ^{[2
]}

Karnataki, Anuradha ^{[1
,3
]}

Gilbert, Luke A. ^{[4
]}

Rome, Michael E. ^{[4
]}

Feagin, Jean E. ^{[1
,3
]}

Bradley, Peter J. ^{[4
]}

Parsons, Marilyn ^{[1
,3
]}

机构：

[1] Seattle Biomed Res Inst, Seattle, WA 98109 USA

[2] Johns Hopkins Univ, Bloomberg Sch Publ Hlth, Dept Mol Microbiol & Immunol, Baltimore, MD 21205 USA

[3] Univ Washington, Dept Global Hlth, Interdisciplinary Program Pathobiol, Seattle, WA 98195 USA

[4] Univ Calif Los Angeles, Dept Microbiol Mol Genet & Immunol, Los Angeles, CA 90095 USA

来源：

EUKARYOTIC CELL | 2008年 / 7卷 / 09期

基金：

英国惠康基金;

关键词：

D O I：

10.1128/EC.00081-08

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Toxoplasma gondii, which causes toxoplasmic encephalitis and birth defects, contains an essential chloroplast-related organelle to which proteins are trafficked via the secretory system. This organelle, the apicoplast, is bounded by multiple membranes. In this report we identify a novel apicoplast-associated thioredoxin family protein, ATrx1, which is predominantly soluble or peripherally associated with membranes, and which localizes primarily to the outer compartments of the organelle. As such, it represents the first protein to be identified as residing in the apicoplast intermembrane spaces. ATrx1 lacks the apicoplast targeting sequences typical of luminal proteins. However, sequences near the N terminus are required for proper targeting of ATrx1, which is proteolytically processed from a larger precursor to multiple smaller forms. This protein reveals a population of vesicles, hitherto unrecognized as being highly abundant in the cell, which may serve to transport proteins to the apicoplast.

引用

页码：1518 / 1529

页数：12

共 54 条

[1] Proteomics gives insight into the regulatory function of chloroplast thioredoxins [J].