|Additional remarks phenotype|
The mutant expresses a C-terminal triple-HA-tagged version of the protein. The endogenous gene has been tagged with the triple-HA tag using a PlasmoGEM construct.
No expression in schizonts detected by IFA or Western Blotting.
This protein was selected in a study aimed at determining the repertoire of DHHC-CRD S-acyl transferase protein family as putative candidates for protein S-acyl transferases (PATs). The genes encoding these proteins were targeted for deletion to analyse their essentiality for blood stages In addition, mutants were generated that express a HA-tagged version of the protein to identify its cellular location
The transgenic parasite has not been cloned and the phenotype of the gene deletion mutant has not been not analysed in detail
Protein palmitoylation in particular is a fundamental, dynamic, and widespread posttranslational mechanism that controls transport, properties and activity of proteins across eukaryotes. Unlike other irreversible lipid modifications such as myristoylation and prenylation, the addition of a 16-carbon saturated palmitate group to the sulfhydryl group of a cysteine to form a hydroxylamine-sensitive thioester linkage, is a reversible modification. This constitutes a fast and dynamic mechanism to spatiotemporally control protein function by impacting reversibly on protein trafficking, stability and clustering. While palmitoylation frequently facilitates membrane association of a soluble protein by the addition of a hydrophobic anchor, this modification also occurs on transmembrane proteins, involving other effects such as structural conformation changes, protein-protein interactions or the clustering to specific lipid domains leading, for example, to assembly of signalling complexes.
Palmitoylation can control the affinity of a protein for lipid membranes, which allows it to impact protein trafficking, stability, folding, signalling and interactions. The publication of the palmitome of the schizont stage of P. falciparum implicated a role for palmitoylation in host cell invasion, protein export and organelle biogenesis.
The enzymes mediating transfer of palmitate from palmitoyl-CoA to a protein substrate were first identified in Saccharomyces cerevisiae and subsequently in mammals. Protein S-acyl transferases (PATs) belong to the DHHC family of proteins that exhibit a catalytic Asp-His-His-Cys conserved motif located within a cysteine-rich domain (CRD) and frequently between two transmembrane regions, facing the cytosol. Substrate recognition and catalysis occur after the protein substrates have associated with membrane via another lipidation.
Search the RMgm-databese for the text term DHHC-CRD for a number of other related mutants