Osborne, Andrew R. and Speicher, K.D. and Tamez, P.A. and Bhattacharjee, S. and Speicher, D.W. and Haldar, K. (2010) The host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum. Molecular and Biochemical Parasitology 171 (1), pp. 25-31. ISSN 0166-6851.
Abstract
During the blood stage of its lifecycle, the malaria parasite resides and replicates inside a membrane vacuole within its host cell, the human erythrocyte. The parasite exports many proteins across the vacuole membrane and into the host cell cytoplasm. Most exported proteins are characterized by the presence of a host targeting (HT) motif, also referred to as a Plasmodium export element (PEXEL), which corresponds to the consensus sequence RxLxE/D/Q. During export the HT motif is cleaved by an unknown protease. Here, we generate parasite lines expressing HT motif containing proteins that are localized to different compartments within the parasite or host cell. We find that the HT motif in a protein that is retained in the parasite endoplasmic reticulum is cleaved and N-acetylated as efficiently as a protein that is exported. This shows that cleavage of the HT motif occurs early in the secretory pathway, in the parasite endoplasmic reticulum.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | Plasmodium, Protein export, Protease, Acetylation |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 20 May 2013 12:12 |
| Last Modified: | 02 Aug 2023 17:04 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/6908 |
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