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Chem Biol. 2011 Jun 24;18(6):711-21. doi: 10.1016/j.chembiol.2011.04.010.

Functional characterization of a SUMO deconjugating protease of Plasmodium falciparum using newly identified small molecule inhibitors.

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1
Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Abstract

Small ubiquitin-related modifier (SUMO) is implicated in the regulation of numerous biological processes including transcription, protein localization, and cell cycle control. Protein modification by SUMO is found in Plasmodium falciparum; however, its role in the regulation of the parasite life cycle is poorly understood. Here we describe functional studies of a SUMO-specific protease (SENP) of P. falciparum, PfSENP1 (PFL1635w). Expression of the catalytic domain of PfSENP1 and biochemical profiling using a positional scanning substrate library demonstrated that this protease has unique cleavage sequence preference relative to the human SENPs. In addition, we describe a class of small molecule inhibitors of this protease. The most potent lead compound inhibited both recombinant PfSENP1 activity and P. falciparum replication in infected human blood. These studies provide valuable new tools for the study of SUMOylation in P. falciparum.

PMID:
21700207
PMCID:
PMC3131532
DOI:
10.1016/j.chembiol.2011.04.010
[Indexed for MEDLINE]
Free PMC Article

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