Abstract:
:For proliferation, the malaria parasite Plasmodium falciparum needs to modify the infected host cell extensively. To achieve this, the parasite exports proteins containing a Plasmodium export element (PEXEL) into the host cell. Phosphatidylinositol-3-phosphate binding and cleavage of the PEXEL are thought to mediate protein export. We show that these requirements can be bypassed, exposing a second level of export control in the N terminus generated after PEXEL cleavage that is sufficient to distinguish exported from nonexported proteins. Furthermore, this region also corresponds to the export domain of a second group of exported proteins lacking PEXELs (PNEPs), indicating shared export properties among different exported parasite proteins. Concordantly, export of both PNEPs and PEXEL proteins depends on unfolding, revealing translocation as a common step in export. However, translocation of transmembrane proteins occurs at the parasite plasma membrane, one step before translocation of soluble proteins, indicating unexpectedly complex translocation events at the parasite periphery.
journal_name
Cell Host Microbejournal_title
Cell host & microbeauthors
Grüring C,Heiber A,Kruse F,Flemming S,Franci G,Colombo SF,Fasana E,Schoeler H,Borgese N,Stunnenberg HG,Przyborski JM,Gilberger TW,Spielmann Tdoi
10.1016/j.chom.2012.09.010subject
Has Abstractpub_date
2012-11-15 00:00:00pages
717-29issue
5eissn
1931-3128issn
1934-6069pii
S1931-3128(12)00349-6journal_volume
12pub_type
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