Unknown

Dataset Information

0

Molecular dissection of novel trafficking and processing of the Toxoplasma gondii rhoptry metalloprotease toxolysin-1.


ABSTRACT: Toxoplasma 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?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 (TLN1). Through genetic ablation and molecular dissection of TLN1, 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, TLN1 undergoes a C-terminal cleavage event that occurs at a processing site not previously seen in Toxoplasma 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 TLN1 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.

SUBMITTER: Hajagos BE 

PROVIDER: S-EPMC3375832 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular dissection of novel trafficking and processing of the Toxoplasma gondii rhoptry metalloprotease toxolysin-1.

Hajagos Bettina E BE   Turetzky Jay M JM   Peng Eric D ED   Cheng Stephen J SJ   Ryan Christopher M CM   Souda Puneet P   Whitelegge Julian P JP   Lebrun Maryse M   Dubremetz Jean-Francois JF   Bradley Peter J PJ  

Traffic (Copenhagen, Denmark) 20111129 2


Toxoplasma gondii utilizes specialized secretory organelles called rhoptries to invade and hijack its host cell. Many rhoptry proteins are proteolytically processed at a highly conserved SΦXE 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 (TLN1). Through genetic ablation and molecular dissection of TLN1, we have identified  ...[more]

Similar Datasets

| S-EPMC3946946 | biostudies-literature
| S-EPMC2532663 | biostudies-literature
| S-EPMC2670854 | biostudies-literature
| S-EPMC6369123 | biostudies-literature
| S-EPMC4959664 | biostudies-literature
| S-EPMC1797617 | biostudies-literature
| S-EPMC10774369 | biostudies-literature
| S-EPMC4863586 | biostudies-other
| S-EPMC3019779 | biostudies-literature
2021-05-13 | PXD018056 | Pride