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Characterization of the 26S proteasome network in Plasmodium falciparum

Academic Article
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Overview

authors

  • Wang, L.
  • Delahunty, C.
  • Fritz-Wolf, K.
  • Rahlfs, S.
  • Prieto, J. H.
  • Yates III, John
  • Becker, K.

publication date

  • December 2015

journal

  • Scientific Reports  Journal

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.

subject areas

  • Antimalarials
  • Chromatography, Affinity
  • Cross-Linking Reagents
  • Enzyme Inhibitors
  • Erythrocytes
  • Formaldehyde
  • Humans
  • Multiprotein Complexes
  • Plasmodium falciparum
  • Proteasome Endopeptidase Complex
  • Protein Structure, Tertiary
  • Proteomics
  • Protozoan Proteins
  • Receptors, Cell Surface
  • Structural Homology, Protein
  • Ubiquitin
  • Ubiquitin-Specific Proteases
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Identity

PubMed Central ID

  • PMC4671066

International Standard Serial Number (ISSN)

  • 2045-2322

Digital Object Identifier (DOI)

  • 10.1038/srep17818

PubMed ID

  • 26639022
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Additional Document Info

start page

  • 17818

volume

  • 5

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