The role of palmitoylation for protein recruitment to the inner membrane complex of the malaria parasite
| Autor: | Susann Herrmann, Maya Kono, Lakshmipuram S. Swapna, Tim W. Gilberger, Sidharth Saini, Louisa Wilcke, Srinivas Nellimarla, Christian Ungermann, Laura Biller, Arun T. John Peter, Johanna Wetzel, Tatianna Wai Ying Wong, Karen L. Mossman, Tobias Spielmann, Olivia Ramsay, Dhaneswar Prusty, Ana Cabrera, Dorothee Heincke, John Parkinson |
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| Rok vydání: | 2014 |
| Předmět: |
DNA Mutational Analysis
Green Fluorescent Proteins Plasmodium falciparum Protozoan Proteins Biotin Biochemistry Catalysis Schizogony Protein acylation Palmitoylation parasitic diseases Humans Palmitoyl acyltransferase Molecular Biology Phylogeny Myristoylation Inner membrane complex biology fungi Cell Membrane food and beverages Membrane Proteins Cell Biology biology.organism_classification Actins Cell biology Malaria Protein Structure Tertiary Protein Transport lipids (amino acids peptides and proteins) Cytokinesis Acyltransferases |
| Zdroj: | The Journal of biological chemistry. 290(3) |
| ISSN: | 1083-351X |
| Popis: | To survive and persist within its human host, the malaria parasite Plasmodium falciparum utilizes a battery of lineage-specific innovations to invade and multiply in human erythrocytes. With central roles in invasion and cytokinesis, the inner membrane complex, a Golgi-derived double membrane structure underlying the plasma membrane of the parasite, represents a unique and unifying structure characteristic to all organisms belonging to a large phylogenetic group called Alveolata. More than 30 structurally and phylogenetically distinct proteins are embedded in the IMC, where a portion of these proteins displays N-terminal acylation motifs. Although N-terminal myristoylation is catalyzed co-translationally within the cytoplasm of the parasite, palmitoylation takes place at membranes and is mediated by palmitoyl acyltransferases (PATs). Here, we identify a PAT (PfDHHC1) that is exclusively localized to the IMC. Systematic phylogenetic analysis of the alveolate PAT family reveals PfDHHC1 to be a member of a highly conserved, apicomplexan-specific clade of PATs. We show that during schizogony this enzyme has an identical distribution like two dual-acylated, IMC-localized proteins (PfISP1 and PfISP3). We used these proteins to probe into specific sequence requirements for IMC-specific membrane recruitment and their interaction with differentially localized PATs of the parasite. |
| Databáze: | OpenAIRE |
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