In Saccharomyces cerevisiae, the effect of H2O2 on ATP, but not on glyceraldehyde-3-phosphate dehydrogenase, depends on the glucose concentration

Archives of Microbiology

Volumn 181, Issue 3, 2004, Pages 231-236

  Osório, Hugo ^a,b   Moradas Ferreira, Pedro ^b   Günther Sillero, María A ^a   Sillero, Antonio ^a  

^a INSTITUTO DE INVESTIGACIONES BIOMÉDICAS ALBERTO SOLS   (Spain)

^b UNIVERSITY OF PORTO   (Portugal)

Author keywords

ATP; Glyceraldehyde 3 phosphate dehydrogenase; H2O2; Inosine; Oxidative stress; Saccharomyces cerevisiae

Indexed keywords

ADENOSINE TRIPHOSPHATE; CATALASE; GLUCOSE; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HYDROGEN PEROXIDE; SUPEROXIDE DISMUTASE;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; FUNGUS GROWTH; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; YEAST CELL;

ADENOSINE TRIPHOSPHATE; CATALASE; GLUCOSE; GLUTATHIONE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HYDROGEN PEROXIDE; INOSINE; KINETICS; NUCLEOTIDES; OXIDANTS; SACCHAROMYCES CEREVISIAE; SUPEROXIDE DISMUTASE;

FUNGI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 1542373519     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-004-0648-6     Document Type: Article

References (30)

1. Atkinson DE (1966) The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7:4030-4034
2. Bergmeyer HU, Bergmeyer J, Grassl M (1983) Methods of enzymatic analysis, vol II, 3rd edn. Verlag Chemie, Weinheim, Germany
3. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
4. Cabiscol E, Piulats E, Echave P, Herrero E, Ros J (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275:27393-27398
5. Chaput M, Brygier J, Lion Y, Sels A (1983) Potentiation of oxygen toxicity by menadione in Saccharomyces cerevisiae. Biochimie 65:501-512
6. 2-induced block of glycolysis as an active ADP-ribosylation reaction protecting cells from apoptosis. FASEB J 14:2266-2276
7. Costa VM, Amorim MA, Quintanilha A, Moradas-Ferreira P (2002) Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: the involvement of the oxidative stress response regulators Yap1 and Skn7. Free Radic Biol Med 33:1507-1515
8. Danshina PV, Schmalhausen EV, Avetisyan AV, Muronetz VI (2001) Mildly oxidized glyceraldehyde-3-phosphate dehydrogenase as a possible regulator of glycolysis. IUBMB Life 51: 309-314
9. Del Rio LA, Sandalio LM, Palma JM, Bueno P, Corpas FJ (1992) Metabolism of oxygen radicals in peroxisomes and cellular implications. Free Radic Biol Med 13:557-580
10. Flohe L, Otting F (1984) Superoxide dismutase assays. Methods Enzymol 105:93-104
11. Gancedo JM (1998) Yeast carbon catabolite repression. Microbiol Mol Biol Rev 62:334-361
12. Gancedo JM, Gancedo C (1986) Catabolite repression mutants of yeast. FEMS Microbiol Rev 32:179-197
13. 2 stimulon in Saccharomyces cerevisiae. J Biol Chem 273:22480-22489
14. Grant CM, Quinn KA, Dawes IW (1999) Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress. Mol Cell Biol 19:2650-2656
15. Horiguchi H, Yurimoto H, Goh T, Nakagawa T, Kato N, Sakai Y (2001) Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance. J Bacteriol 183:6372-6383
16. Lin SJ, Defossez PA, Guarente L (2000) Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289:2126-2128
17. Lin SJ, Kaeberlein M, Andalis, AA, Sturtz LA, Defossez PA, Culotta VC, Fink GR, Guarente L (2002) Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418:344-348
18. McAlister L, Holland MJ (1985) Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260:15019-15027
19. 2, but not menadione, provokes a decrease in the ATP and an increase in the inosine levels in Saccharomyces cerevisiae. An experimental and theoretical approach. Eur J Biochem 270:1578-1589
20. Pernambuco MB, Winderickx J, Crauwels M, Griffioen G, Mager WH, Thevelein JM (1996) Glucose-triggered signalling in Saccharomyces cerevisiae: different requirements for sugar phosphorylation between cells grown on glucose and those grown on non-fermentable carbon sources. Microbiology 142:1775-1782
21. Pronk JT, Yde Steensma H, Van Dijken JP (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12:1607-1633
22. Ribeiro JM, Juzgado D, Crespo E, Sillero A (1990) Computer program for the reservoir model of metabolic crossroads. Comput Biol Med 20:35-46
23. Rytka J, Sledziewski A, Lukaszkiewicz J, Bilinski T (1978) Haemoprotein formation in yeast. III. The role of carbon catabolite repression in the regulation of catalase A and T formation. Mol Gen Genet 160:51-57
24. Shenton D, Grant CM (2003) Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 374 (Pt2):513-519
25. Shenton D, Perrone G, Quinn KA, Dawes IW, Grant CM (2002) Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae. J Biol Chem 277:16853-16859
26. 4A), ATP and catecholamine content in bovine adrenal medulla, chromaffin granules and chromaffin cells. Biochimie 76:404-409
27. Thomas BJ, Rothstein R (1989) Elevated recombination rates in transcriptionally active DNA. Cell 56:619-630
28. Weibel KE, Mor JR, Fiechter A (1974) Rapid sampling of yeast cells and automated assays of adenylate, citrate, pyruvate and glucose-6-phosphate pools. Anal Biochem 58:208-216
29. Westerbeek-Marres CA, Moore MM, Autor AP (1988) Regulation of manganese superoxide dismutase in Saccharomyces cerevisiae. The role of respiratory chain activity. Eur J Biochem 174:611-620
30. Zhou M, Diwu Z, Panchuk-Voloshina N, Haugland RP (1997) A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal Biochem 253:162-168