Targeting of the ring exported protein 1 to the Maurer's Clefts is mediated by a two-phase process

Dixon, Matthew W. A., Hawthorne, Paula L., Spielmann, Tobias, Anderson, Karen L., Trenholme, Katharine R. and Gardiner, Donald L. (2008) Targeting of the ring exported protein 1 to the Maurer's Clefts is mediated by a two-phase process. Traffic, 9 8: 1316-1326. doi:10.1111/j.1600-0854.2008.00768.x


Author Dixon, Matthew W. A.
Hawthorne, Paula L.
Spielmann, Tobias
Anderson, Karen L.
Trenholme, Katharine R.
Gardiner, Donald L.
Title Targeting of the ring exported protein 1 to the Maurer's Clefts is mediated by a two-phase process
Journal name Traffic   Check publisher's open access policy
ISSN 1398-9219
Publication date 2008-08
Year available 2008
Sub-type Article (original research)
DOI 10.1111/j.1600-0854.2008.00768.x
Volume 9
Issue 8
Start page 1316
End page 1326
Total pages 11
Editor F. M. Brodsky
M. C. P. Marsh
Place of publication Denmark
Publisher Wiley-Blackwell Munksgaard
Collection year 2009
Language eng
Subject C1
970111 Expanding Knowledge in the Medical and Health Sciences
110803 Medical Parasitology
Abstract Early development of Plasmodium falciparum within the erythrocyte is characterized by the large-scale export of proteins to the host cell. In many cases, export is mediated by a short sequence called the Plasmodium export element (PEXEL) or vacuolar transport signal; however, a number of previously characterized exported proteins do not contain such an element. In this study, we investigated the mechanisms of export of the PEXEL-negative ring exported protein 1 (REX1). This protein localizes to the Maurer's clefts, parasite-induced structures in the host-cell cytosol. Transgenic parasites expressing green fluorescent protein–REX1 chimeras revealed that the single hydrophobic stretch plus an additional 10 amino acids mediate the export of REX1. Biochemical characterization of these chimeras indicated that REX1 was exported as a soluble protein. Inclusion of a sequence containing a predicted coiled-coil motif led to the correct localization of REX1 at the Maurer's clefts, suggesting that association with the clefts occurs at the final stage of protein export only. These results indicate that PEXEL-negative exported proteins can be exported in a soluble state and that sequences without any apparent resemblance to a PEXEL motif can mediate export across the parasitophorous vacuole membrane.
Formatted abstract
Early development of Plasmodium falciparum within the erythrocyte is characterized by the large-scale export of proteins to the host cell. In many cases, export is mediated by a short sequence called the Plasmodium export element (PEXEL) or vacuolar transport signal; however, a number of previously characterized exported proteins do not contain such an element. In this study, we investigated the mechanisms of export of the PEXEL-negative ring exported protein 1 (REX1). This protein localizes to the Maurer's clefts, parasite-induced structures in the host-cell cytosol. Transgenic parasites expressing green fluorescent protein–REX1 chimeras revealed that the single hydrophobic stretch plus an additional 10 amino acids mediate the export of REX1. Biochemical characterization of these chimeras indicated that REX1 was exported as a soluble protein. Inclusion of a sequence containing a predicted coiled-coil motif led to the correct localization of REX1 at the Maurer's clefts, suggesting that association with the clefts occurs at the final stage of protein export only. These results indicate that PEXEL-negative exported proteins can be exported in a soluble state and that sequences without any apparent resemblance to a PEXEL motif can mediate export across the parasitophorous vacuole membrane.
Keyword host-cell remodelling
Malaria
Maurer's Clefts
PEXEL
Ring Stage
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
School of Medicine Publications
 
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Created: Mon, 06 Apr 2009, 16:44:45 EST by Amanda Jones on behalf of School of Medicine