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- W1507598208 abstract "T oxoplasma gondii utilizes specialized secretory organelles called rhoptries to invade and hijack its host cell. Many rhoptry proteins are proteolytically processed at a highly conserved S Φ XE site to remove organellar targeting sequences that may also affect protein activity. We have studied the trafficking and biogenesis of a secreted rhoptry metalloprotease with homology to insulysin that we named toxolysin‐1 ( TLN 1). Through genetic ablation and molecular dissection of TLN 1, we have identified the smallest rhoptry targeting domain yet reported and expanded the consensus sequence of the rhoptry pro‐domain cleavage site. In addition to removal of its pro‐domain, TLN 1 undergoes a C ‐terminal cleavage event that occurs at a processing site not previously seen in T oxoplasma rhoptry proteins. While pro‐domain cleavage occurs in the nascent rhoptries, processing of the C ‐terminal region precedes commitment to rhoptry targeting, suggesting that it is mediated by a different maturase, and we have identified residues critical for proteolysis. We have additionally shown that both pieces of TLN 1 associate in a detergent‐resistant complex, formation of which is necessary for trafficking of the C ‐terminal portion to the rhoptries. Together, these studies reveal novel processing and trafficking events that are present in the protein constituents of this unusual secretory organelle." @default.
- W1507598208 created "2016-06-24" @default.
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- W1507598208 date "2011-11-29" @default.
- W1507598208 modified "2023-10-15" @default.
- W1507598208 title "Molecular Dissection of Novel Trafficking and Processing of the <i><scp>T</scp>oxoplasma gondii</i> Rhoptry Metalloprotease Toxolysin‐1" @default.
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- W1507598208 doi "https://doi.org/10.1111/j.1600-0854.2011.01308.x" @default.
- W1507598208 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3375832" @default.
- W1507598208 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22035499" @default.
- W1507598208 hasPublicationYear "2011" @default.
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