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Verfasst von:Rhiel, Manuel [VerfasserIn]   i
 Lanzer, Michael [VerfasserIn]   i
 Sanchez, Cecilia P. [VerfasserIn]   i
Titel:Trafficking of the exported P. falciparum chaperone PfHsp70x
Verf.angabe:Manuel Rhiel, Verena Bittl, Anke Tribensky, Sarah C. Charnaud, Maja Strecker, Sebastian Müller, Michael Lanzer, Cecilia Sanchez, Christine Schaeffer-Reiss, Benoit Westermann, Brendan S. Crabb, Paul R. Gilson, Simone Külzer & Jude M. Przyborski
E-Jahr:2016
Jahr:08 November 2016
Umfang:13 S.
Teil:volume:6
 year:2016
 extent:13
Fussnoten:Gesehen am 21.10.2021
Titel Quelle:Enthalten in: Scientific reports
Ort Quelle:[London] : Macmillan Publishers Limited, part of Springer Nature, 2011
Jahr Quelle:2016
Band/Heft Quelle:6(2016) Artikel-Nummer 36174, 13 Seiten
ISSN Quelle:2045-2322
Abstract:Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.
DOI:doi:10.1038/srep36174
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1038/srep36174
 Volltext: https://www.nature.com/articles/srep36174
 DOI: https://doi.org/10.1038/srep36174
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1745201432
Verknüpfungen:→ Zeitschrift

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