Polysome profiling reveals translational control of gene expression in the human malaria parasite Plasmodium falciparum.

Background: In eukaryotic organisms, gene expression is regulated at multiple levels during the processes of transcription and translation. The absence of a tight regulatory network for transcription in the human malaria parasite suggests that gene expression may largely be controlled at post-transcriptional and translational levels.

Results: In this study, we compare steady-state mRNA and polysome-associated mRNA levels of Plasmodium falciparum at different time points during its asexual cell cycle.

Targeting the Plasmodium ubiquitin/proteasome system with anti-malarial compounds: promises for the future.

The human malarial parasite, Plasmodium falciparum, is responsible for one of the most infectious diseases of the world and is quickly gaining resistance to the commonly used antimalarial treatments. New data are continually reinforcing the idea that biological functions associated with the ubiquitin proteasome system (UPS) are not just limited to non-lysomal degradation of proteins but consist of a wide array of regulatory mechanisms such as cell cycle progression, transcriptional regulation, gene expression and trafficking. While there is much effort in understanding the UPS in many eukaryotic organisms, the Plasmodium UPS has been relatively understudied despite its potential as a therapeutic drug target.

Post-translational modifications in Plasmodium: more than you think!

Recent evidences indicate that transcription in Plasmodium may be hard-wired and rigid, deviating from the classical model of transcriptional gene regulation. Thus, it is important that other regulatory pathways be investigated as a comprehensive effort to curb the deadly malarial parasite. Research in post-translational modifications in Plasmodium is an emerging field that may provide new venues for drug discovery and potential new insights into how parasitic protozoans regulate their life cycle.

Deciphering the ubiquitin-mediated pathway in apicomplexan parasites: a potential strategy to interfere with parasite virulence.

Background: Reversible modification of proteins through the attachment of ubiquitin or ubiquitin-like modifiers is an essential post-translational regulatory mechanism in eukaryotes. The conjugation of ubiquitin or ubiquitin-like proteins has been demonstrated to play roles in growth, adaptation and homeostasis in all eukaryotes, with perturbation of ubiquitin-mediated systems associated with the pathogenesis of many human diseases, including cancer and neurodegenerative disorders.

Methodology/principal Findings: Here we describe the use of an HMM search of functional Pfam domains found in the key components of the ubiquitin-mediated pathway necessary to activate and reversibly modify target proteins in eight apicomplexan parasitic protozoa for which complete or late-stage genome projects exist.