histone methylase KMTox interacts with the redox-sensor peroxiredoxin-1 and targets genes involved in Toxoplasma gondii antioxidant defences

The ability of living cells to alter their gene expression patterns in response to environmental changes is essential for viability. Oxidative stress represents a common threat for all aerobic life. In normally growing cells, in which hydrogen peroxide generation is transient or pulsed, the antioxid...

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Published in:Molecular microbiology 2009, Vol.71 (1), p.212-226
Main Authors: Sautel, Céline F, Ortet, Philippe, Saksouk, Nehmé, Kieffer, Sylvie, Garin, Jérôme, Bastien, Olivier, Hakimi, Mohamed-Ali
Format: Article
Language:English
Subjects:
Animals
Antioxidants
Biochemistry, Molecular Biology
Biological and medical sciences
Chromatin
Chromatin Immunoprecipitation
Fundamental and applied biological sciences. Psychology
Gene expression
Gene Expression Regulation
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Histones - metabolism
Hydrogen Peroxide - pharmacology
Life Sciences
Microbiology
Oxidation
Oxidative Stress
Parasitic protozoa
Peroxiredoxins - metabolism
Proteins
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
RNA, Protozoan - genetics
Toxoplasma - drug effects
Toxoplasma - enzymology
Toxoplasma - genetics
Toxoplasma gondii
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Summary:The ability of living cells to alter their gene expression patterns in response to environmental changes is essential for viability. Oxidative stress represents a common threat for all aerobic life. In normally growing cells, in which hydrogen peroxide generation is transient or pulsed, the antioxidant systems efficiently control its concentration. Intracellular parasites must also protect themselves against the oxidative burst imposed by the host. In this work, we have investigated the role of KMTox, a new histone lysine methyltransferase, in the obligate intracellular parasite Toxoplasma gondii. KMTox is a nuclear protein that holds a High Mobility Group domain, which is thought to recognize bent DNA. The enzyme methylates both histones H4 and H2A in vitro with a great preference for the substrate in reduced conditions. Importantly, KMTox interacts specifically with the typical 2-cys peroxiredoxin-1 and the binding is to some extent enhanced upon oxidation. It appears that the cellular functions that are primarily regulated by the KMTox are antioxidant defences and maintenance of cellular homeostasis. KMTox may regulate gene expression in T. gondii by providing the rapid re-arrangement of chromatin domains and by interacting with the redox-sensor TgPrx1 contribute to establish the antioxidant 'firewall' in T. gondii.
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2008.06519.x