A Genome-wide Chromatin-associated Nuclear Peroxiredoxin from the Malaria Parasite Plasmodium falciparum
Details
Publication Year 2011-04-01, Volume 286, Issue #13, Page 11746-11755
Journal Title
JOURNAL OF BIOLOGICAL CHEMISTRY
Publication Type
Journal Article
Abstract
Malaria parasites are subjected to high levels of oxidative stress during their development inside erythrocytes and the ability of the parasite to defend itself against this assault is critical to its survival. Therefore, Plasmodium possesses an effective antioxidant defense system that could potentially be used as a target for the development of inhibitor-based therapy. We have identified an unusual peroxiredoxin protein that localizes to the nucleus of Plasmodium falciparum and have renamed it Pfn Prx (PF10_0268, earlier called MCP1). Our work reveals that Pfn Prx has a broad specificity of substrate being able to utilize thioredoxin and glutaredoxin as reductants and having the ability to reduce simple and complex peroxides. Intriguingly, chromatin immunoprecipitation followed by deep sequencing reveals that the enzyme associates with chromatin in a genome-wide manner with a slight enrichment in coding regions. Our results represent the first description of a dedicated chromatin-associated peroxiredoxin and potentially represent an ingenious way by which the parasite can survive the highly oxidative environment within its human host.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Keywords
INFECTED ERYTHROCYTES; THIOREDOXIN PEROXIDASES; ANTIOXIDANT SYSTEMS; OXIDATIVE STRESS; HISTONE H1; PROTEIN; REDOX; INVASION; DOMAIN; TRAFFICKING
Rights Notice
Refer to copyright notice on published article.


Creation Date: 2011-04-01 12:00:00
Last Modified: 0001-01-01 12:00:00
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