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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 TimWolf,
Spielmann Tobias
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06582.x
Subject(s) - biology , transmembrane domain , transmembrane protein , plasmodium falciparum , microbiology and biotechnology , peptide sequence , virulence , genetics , computational biology , amino acid , gene , malaria , receptor , immunology
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.