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Sequence requirements for the export of the Plasmodium falciparum Maurer's clefts protein REX2

Haase, Silvia, Herrmann, Susann, Grüring, Christof, Heiber, Arlett, Jansen, Pascal W., Langer, Christine, Treeck, Moritz, Cabrera, Ana, Bruns, Caroline, Struck, Nicole S., Kono, Maya, Engelberg, Klemens, Ruch, Ulrike, Stunnenberg, Hendrik G., Gilberger, Tim-Wolf and Spielmann, Tobias 2009, Sequence requirements for the export of the Plasmodium falciparum Maurer's clefts protein REX2, Molecular microbiology, vol. 71, no. 4, pp. 1003-1017, doi: 10.1111/j.1365-2958.2008.06582.x.

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Title Sequence requirements for the export of the Plasmodium falciparum Maurer's clefts protein REX2
Author(s) Haase, Silvia
Herrmann, Susann
Grüring, Christof
Heiber, Arlett
Jansen, Pascal W.
Langer, Christine
Treeck, Moritz
Cabrera, Ana
Bruns, Caroline
Struck, Nicole S.
Kono, Maya
Engelberg, Klemens
Ruch, Ulrike
Stunnenberg, Hendrik G.
Gilberger, Tim-Wolf
Spielmann, Tobias
Journal name Molecular microbiology
Volume number 71
Issue number 4
Start page 1003
End page 1017
Publisher Wiley-Blackwell Publishing
Place of publication Oxford, England
Publication date 2009-02
ISSN 0950-382X
1365-2958
Summary A short motif termed Plasmodium export element (PEXEL) or vacuolar targeting signal (VTS) characterizes Plasmodium proteins exported into the host cell. These proteins mediate host cell modifications essential for parasite survival and virulence. However, several PEXEL-negative exported proteins indicate that the currently predicted malaria exportome is not complete and it is unknown whether and how these proteins relate to PEXEL-positive export. Here we show that the N-terminal 10 amino acids of the PEXEL-negative exported protein REX2 (ring-exported protein 2) are necessary for its targeting and that a single-point mutation in this region abolishes export. Furthermore we show that the REX2 transmembrane domain is also essential for export and that together with the N-terminal region it is sufficient to promote export of another protein. An N-terminal region and the transmembrane domain of the unrelated PEXEL-negative exported protein SBP1 (skeleton-binding protein 1) can functionally replace the corresponding regions in REX2, suggesting that these sequence features are also present in other PEXEL-negative exported proteins. Similar to PEXEL proteins we find that REX2 is processed, but in contrast, detect no evidence for N-terminal acetylation.
Language eng
DOI 10.1111/j.1365-2958.2008.06582.x
Field of Research 110803 Medical Parasitology
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2008, The Authors
Persistent URL http://hdl.handle.net/10536/DRO/DU:30040962

Document type: Journal Article
Collection: School of Medicine
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