Journal article

Publication year: 2015

Pages: 17818-

Journal: Scientific Reports

Volume number: 5

ISSN: 2045-2322

eISSN: 2045-2322

Open access status: Gold

DOI Link: https://doi.org/10.1038/srep17818

Publisher: Nature Research

Abstract: 
In eukaryotic cells, the ubiquitin-proteasome system as a key regulator of protein quality control is an excellent drug target. We therefore aimed to analyze the 26S proteasome complex in the malaria parasite Plasmodium falciparum, which still threatens almost half of the world's population. First, we established an affinity purification protocol allowing for the isolation of functional 26S proteasome complexes from the parasite. Subunit composition of the proteasome and component stoichiometry were studied and physiologic interacting partners were identified via in situ protein crosslinking. Furthermore, intrinsic ubiquitin receptors of the plasmodial proteasome were determined and their roles in proteasomal substrate recognition were analyzed. Notably, PfUSP14 was characterized as a proteasome-associated deubiquitinase resulting in the concept that targeting proteasomal deubiquitinating activity in P. falciparum may represent a promising antimalarial strategy. The data provide insights into a profound network orchestrated by the plasmodial proteasome and identified novel drug target candidates in the ubiquitin-proteasome system.

Harvard Citation style: Wang, L., Delahunty, C., Fritz-Wolf, K., Rahlfs, S., Prieto, J., Yates, J., et al. (2015) Characterization of the 26S proteasome network in Plasmodium falciparum, Scientific Reports, 5, p. 17818. https://doi.org/10.1038/srep17818

APA Citation style: Wang, L., Delahunty, C., Fritz-Wolf, K., Rahlfs, S., Prieto, J., Yates, J., & Becker, K. (2015). Characterization of the 26S proteasome network in Plasmodium falciparum. Scientific Reports. 5, 17818. https://doi.org/10.1038/srep17818