Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 6 April 1984:
Vol. 224. no. 4644, pp. 70 - 72
DOI: 10.1126/science.6322306

Articles

Science, Vol 224, Issue 4644, 70-72
Copyright © 1984 by American Association for the Advancement of Science


articles

Entamoeba histolytica: a eukaryote without glutathione metabolism

RC Fahey, GL Newton, B Arrick, T Overdank-Bogart, and SB Aley

Entamoeba histolytica was found to grow normally without producing glutathione and the main enzymes of glutathione metabolism, indicating that glutathione is not essential for many eukaryotic processes. This parasitic amoeba is an unusual eukaryote whose special features may help define the crucial functions of glutathione in those eukaryotes that do use it. Since Entamoeba histolytica lacks mitochondria and the usual aerobic respiratory pathways, the finding that it grows without glutathione and other evidence support the hypothesis that a primary function of glutathione in eukaryotes involves protection against oxygen toxicity associated with mitochondria and suggest that eukaryotes may have acquired glutathione metabolism at the time that they acquired mitochondria.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Mercaptopyruvate Sulfurtransferase of Trichomonas vaginalis Links Cysteine Catabolism to the Production of Thioredoxin Persulfide.
G. D. Westrop, I. Georg, and G. H. Coombs (2009)
J. Biol. Chem. 284, 33485-33494
   Abstract »    Full Text »    PDF »
Current Therapeutics, Their Problems, and Sulfur-Containing-Amino-Acid Metabolism as a Novel Target against Infections by "Amitochondriate" Protozoan Parasites.
V. Ali and T. Nozaki (2007)
Clin. Microbiol. Rev. 20, 164-187
   Abstract »    Full Text »    PDF »
Characterization of the Bifunctional {gamma}-Glutamate-cysteine Ligase/Glutathione Synthetase (GshF) of Pasteurella multocida.
B. Vergauwen, D. De Vos, and J. J. Van Beeumen (2006)
J. Biol. Chem. 281, 4380-4394
   Abstract »    Full Text »    PDF »
Glutathione Synthesis in Streptococcus agalactiae: ONE PROTEIN ACCOUNTS FOR {gamma}-GLUTAMYLCYSTEINE SYNTHETASE AND GLUTATHIONE SYNTHETASE ACTIVITIES.
B. E. Janowiak and O. W. Griffith (2005)
J. Biol. Chem. 280, 11829-11839
   Abstract »    Full Text »    PDF »
Identification and Characterization of Two Isoenzymes of Methionine {gamma}-Lyase from Entamoeba histolytica: A KEY ENZYME OF SULFUR-AMINO ACID DEGRADATION IN AN ANAEROBIC PARASITIC PROTIST THAT LACKS FORWARD AND REVERSE TRANS-SULFURATION PATHWAYS.
M. Tokoro, T. Asai, S. Kobayashi, T. Takeuchi, and T. Nozaki (2003)
J. Biol. Chem. 278, 42717-42727
   Abstract »    Full Text »    PDF »
Drug Targets and Mechanisms of Resistance in the Anaerobic Protozoa.
P. Upcroft and J. A. Upcroft (2001)
Clin. Microbiol. Rev. 14, 150-164
   Abstract »    Full Text »    PDF »
Glutathione synthesis is essential for mouse development but not for cell growth in culture.
Z.-Z. Shi, J. Osei-Frimpong, G. Kala, S. V. Kala, R. J. Barrios, G. M. Habib, D. J. Lukin, C. M. Danney, M. M. Matzuk, and M. W. Lieberman (2000)
PNAS 97, 5101-5106
   Abstract »    Full Text »    PDF »
Characterization of the Gene Encoding Serine Acetyltransferase, a Regulated Enzyme of Cysteine Biosynthesis from the Protist Parasites Entamoeba histolytica and Entamoeba dispar. REGULATION AND POSSIBLE FUNCTION OF THE CYSTEINE BIOSYNTHETIC PATHWAY IN ENTAMOEBA.
T. Nozaki, T. Asai, L. B. Sanchez, S. Kobayashi, M. Nakazawa, and T. Takeuchi (1999)
J. Biol. Chem. 274, 32445-32452
   Abstract »    Full Text »    PDF »
Novel Protein-disulfide Isomerases from the Early-diverging Protist Giardia lamblia.
L. A. Knodler, R. Noiva, K. Mehta, J. M. McCaffery, S. B. Aley, S. G. Svard, T. G. Nystul, D. S. Reiner, J. D. Silberman, and F. D. Gillin (1999)
J. Biol. Chem. 274, 29805-29811
   Abstract »    Full Text »    PDF »
Metronidazole Resistance in the Protozoan Parasite Entamoeba histolytica Is Associated with Increased Expression of Iron-containing Superoxide Dismutase and Peroxiredoxin and Decreased Expression of Ferredoxin 1 and Flavin Reductase.
C. Wassmann, A. Hellberg, E. Tannich, and I. Bruchhaus (1999)
J. Biol. Chem. 274, 26051-26056
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)