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Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants.
FEMS Microbiol Rev. 2005 Sep; 29(4):653-71.FM

Abstract

Glutathione (gamma-glu-cys-gly; GSH) is usually present at high concentrations in most living cells, being the major reservoir of non-protein reduced sulfur. Because of its unique redox and nucleophilic properties, GSH serves in bio-reductive reactions as an important line of defense against reactive oxygen species, xenobiotics and heavy metals. GSH is synthesized from its constituent amino acids by two ATP-dependent reactions catalyzed by gamma-glutamylcysteine synthetase and glutathione synthetase. In yeast, these enzymes are found in the cytosol, whereas in plants they are located in the cytosol and chloroplast. In protists, their location is not well established. In turn, the sulfur assimilation pathway, which leads to cysteine biosynthesis, involves high and low affinity sulfate transporters, and the enzymes ATP sulfurylase, APS kinase, PAPS reductase or APS reductase, sulfite reductase, serine acetyl transferase, O-acetylserine/O-acetylhomoserine sulfhydrylase and, in some organisms, also cystathionine beta-synthase and cystathionine gamma-lyase. The biochemical and genetic regulation of these pathways is affected by oxidative stress, sulfur deficiency and heavy metal exposure. Cells cope with heavy metal stress using different mechanisms, such as complexation and compartmentation. One of these mechanisms in some yeast, plants and protists is the enhanced synthesis of the heavy metal-chelating molecules GSH and phytochelatins, which are formed from GSH by phytochelatin synthase (PCS) in a heavy metal-dependent reaction; Cd(2+) is the most potent activator of PCS. In this work, we review the biochemical and genetic mechanisms involved in the regulation of sulfate assimilation-reduction and GSH metabolism when yeast, plants and protists are challenged by Cd(2+).

Authors+Show Affiliations

Departamento de Bioquímica, Instituto Nacional de Cardiología, Juan Badiano 1, Col. Sección XVI Tlalpan, México. cozatl@hotmail.comNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

16102596

Citation

Mendoza-Cózatl, David, et al. "Sulfur Assimilation and Glutathione Metabolism Under Cadmium Stress in Yeast, Protists and Plants." FEMS Microbiology Reviews, vol. 29, no. 4, 2005, pp. 653-71.
Mendoza-Cózatl D, Loza-Tavera H, Hernández-Navarro A, et al. Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiol Rev. 2005;29(4):653-71.
Mendoza-Cózatl, D., Loza-Tavera, H., Hernández-Navarro, A., & Moreno-Sánchez, R. (2005). Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiology Reviews, 29(4), 653-71.
Mendoza-Cózatl D, et al. Sulfur Assimilation and Glutathione Metabolism Under Cadmium Stress in Yeast, Protists and Plants. FEMS Microbiol Rev. 2005;29(4):653-71. PubMed PMID: 16102596.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. AU - Mendoza-Cózatl,David, AU - Loza-Tavera,Herminia, AU - Hernández-Navarro,Andrea, AU - Moreno-Sánchez,Rafael, PY - 2004/03/24/received PY - 2004/08/03/revised PY - 2004/09/17/accepted PY - 2005/8/17/pubmed PY - 2005/11/8/medline PY - 2005/8/17/entrez SP - 653 EP - 71 JF - FEMS microbiology reviews JO - FEMS Microbiol Rev VL - 29 IS - 4 N2 - Glutathione (gamma-glu-cys-gly; GSH) is usually present at high concentrations in most living cells, being the major reservoir of non-protein reduced sulfur. Because of its unique redox and nucleophilic properties, GSH serves in bio-reductive reactions as an important line of defense against reactive oxygen species, xenobiotics and heavy metals. GSH is synthesized from its constituent amino acids by two ATP-dependent reactions catalyzed by gamma-glutamylcysteine synthetase and glutathione synthetase. In yeast, these enzymes are found in the cytosol, whereas in plants they are located in the cytosol and chloroplast. In protists, their location is not well established. In turn, the sulfur assimilation pathway, which leads to cysteine biosynthesis, involves high and low affinity sulfate transporters, and the enzymes ATP sulfurylase, APS kinase, PAPS reductase or APS reductase, sulfite reductase, serine acetyl transferase, O-acetylserine/O-acetylhomoserine sulfhydrylase and, in some organisms, also cystathionine beta-synthase and cystathionine gamma-lyase. The biochemical and genetic regulation of these pathways is affected by oxidative stress, sulfur deficiency and heavy metal exposure. Cells cope with heavy metal stress using different mechanisms, such as complexation and compartmentation. One of these mechanisms in some yeast, plants and protists is the enhanced synthesis of the heavy metal-chelating molecules GSH and phytochelatins, which are formed from GSH by phytochelatin synthase (PCS) in a heavy metal-dependent reaction; Cd(2+) is the most potent activator of PCS. In this work, we review the biochemical and genetic mechanisms involved in the regulation of sulfate assimilation-reduction and GSH metabolism when yeast, plants and protists are challenged by Cd(2+). SN - 0168-6445 UR - https://www.unboundmedicine.com/medline/citation/16102596/Sulfur_assimilation_and_glutathione_metabolism_under_cadmium_stress_in_yeast_protists_and_plants_ DB - PRIME DP - Unbound Medicine ER -