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That parasite-specific organelle is called the glycosome, which plays a crucial role in cell processes, particularly energy metabolism. The glycosome organelle is surrounded by a single membrane, where several proteins reside. These proteins (Pex13.1, 13.2 and 14) import other proteins required for normal cell functioning.
In their study, Morris and her students used biochemical approaches to partially resolve the composition of those three glycosome proteins. In the process, they demonstrated that Pex13.2 is an integral glycosome membrane protein that interacts with Pex13.1 and Pex14, which was previously not known.
Utilizing the advanced microscopy technology in Clemson's Light Imaging Facility, they also obtained very high-resolution images, and found that Pex13.2 exhibits a unique localization pattern that may be critical to its function.
"No one knew what Pex13.2 was doing, but our study adds to that understanding," said Morris, a member of Clemson's Eukaryotic Pathogens Innovation Center (EPIC). "Now we know that it plays a role in import of proteins and the division of the organelles."
The team also silenced Pex13.2, which resulted in parasites with fewer, larger glycosomes. Without 13.2, the parasite couldn't import glycosome proteins, resulting in the parasite's death.
"Others have shown that when 13.2 is knocked out, the cell dies," said Morris, noting that by fully understanding the organelle's parts and functions, drug companies could someday design rational approaches to disrupting the system and killing the parasite. Source:
Clemson University Journal reference:
Crowe, L.P., et al. (2020) Trypanosoma brucei Pex13.2 Is an Accessory Peroxin That Functions in the Import of Peroxisome Targeting Sequence Type 2 Proteins and Localizes to Subdomains of the Glycosomet. mSphere . doi.org/10.1128/mSphere.00744-19 .
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